Lab Presentation

Structural Biology of Oxidative Stress Systems. From Organelles to Membrane Proteins

The major expertise of the lab is in Macromolecular X-Ray Crystallography. Currently we are especially interested in studies requiring the integration of different structural methodologies with research centered on two biological systems, one prokaryotic and one eukaryotic:

  • The Functional and Structural Study of Mycoplasmas Terminal Organelle
  • The Structure and Interactions of Peroxisomal Proteins

Several targets of our research lines include macromolecular aggregates and membrane-associated or integral membrane proteins. In addition, we also have a number of different collaborative projects mainly related with oxidative-stress processes and pathologies.

Peroxisomal proteins

Projects

there is currently no project published on this page

Lab People

Ignacio Fita Rodriguez

Ignacio Fita Rodriguez

Research Professor CSIC

ifrcri@ibmb.csic.es
+34 934 034 949 / +34 934 034 956

David Aparicio Alarcón

David Aparicio Alarcón

Postdoctoral Researcher

daacri@ibmb.csic.es

David Vizarraga Revuelto

David Vizarraga Revuelto

PhD Student

davcri@ibmb.csic.es

Rosa Perez Luque

Rosa Perez Luque

Research Technician

rplcri@ibmb.csic.es

Alicia Guasch Mitjans

Alicia Guasch Mitjans

Staff scientist

agmcri@ibmb.csic.es

Martin Goethe

Martin Goethe

Postdoctoral Researcher

Selected Publications


Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase.

Aparicio D, Pérez-Luque R, Carpena X, Díaz M, Ferrer JC, Loewen PC, Fita I

J Biol Chem 288: 11907-11919. (2013)


Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa.

Garreta A, Val-Moraes SP, García-Fernández Q, Busquets M, Juan C, Oliver A, Ortiz A, Gaffney BJ, Fita I, Manresa A, Carpena X

FASEB J 27(12):4811-21. (2013)


The EAGR box structure: a motif involved in mycoplasma motility.

Calisto BM, Broto A, Martinelli L, Querol E, Piñol J, Fita I

Mol Microbiol 86: 382-393. (2012)


Crystal structure of Brucella abortus deoxyxylulose-5-phosphate reductoisomerase-like (DRL) enzyme involved in isoprenoid biosynthesis.

Pérez-Gil J, Calisto BM, Behrendt C, Kurz T, Fita I, Rodríguez-Concepción M

J Biol Chem 287: 15803-15809. (2012)


High conformational stability of secreted eukaryotic catalase-peroxidases: answers from first crystal structure and unfolding studies.

Zámocký M, García-Fernández Q, Gasselhuber B, Jakopitsch C, Furtmüller PG, Loewen PC, Fita I, Obinger C, Carpena X

J Biol Chem 287: 32254-32262. (2012)


Molecular basis of substrate-induced permeation by an amino acid antiporter.
Kowalczyk L, Ratera M, Paladino A, Bartoccioni P, Errasti-Murugarren E, Valencia E, Portella G, Bial S, Zorzano A, Fita I, Orozco M, Carpena X, Vázquez-Ibar JL, Palacín M

Proc Natl Acad Sci USA 108: 3935-3940. (2011)


Isonicotinic acid hydrazide conversion to Isonicotinyl-NAD by catalase-peroxidases.
Wiseman B, Carpena X, Feliz M, Donald LJ, Pons M, Fita I, Loewen PC
J Biol Chem 285: 26662-26673. (2010)


The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP.

Querol-Audí J, Casañas A, Usón I, Luque D, Castón JR, Fita I, Verdaguer N

EMBO J 28: 3450-3457. (2009)


Essential role of proximal histidine-asparagine interaction in mammalian peroxidases.

Carpena X, Vidossich P, Schroettner K, Calisto BM, Banerjee S, Stampler J, Soudi M, Furtmüller PG, Rovira C, Fita I, Obinger C

J Biol Chem 284: 25929-25937. (2009)


The structures and electronic configuration of compound I intermediates of Helicobacter pylori and Penicillium vitale catalases determined by X-ray crystallography and QM/MM density functional theory calculations.

Alfonso-Prieto M, Borovik A, Carpena X, Murshudov G, Melik-Adamyan W, Fita I, Rovira C, Loewen PC

J Am Chem Soc 129: 4193-4205. (2007)


Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10.

Gallego O, Ruiz FX, Ardèvol A, Domínguez M, Alvarez R, de Lera AR, Rovira C, Farrés J, Fita I, Parés X

Proc Natl Acad Sci USA 104: 20764-20769. (2007)


The crystal structure of the complex of PII and acetylglutamate kinase reveals how PII controls the storage of nitrogen as arginine.

Llàcer JL, Contreras A, Forchhammer K, Marco-Marín C, Gil-Ortiz F, Maldonado R, Fita I, Rubio V

Proc Natl Acad Sci USA 104: 17644-17649. (2007)


All Publications

Thermal motions in protein: Large effects on the time-averaged interaction energies

M Goethe, I Fita, JM Rubi.

AIP Advances 6, 035020. (2016)


Structure-guided mutations in the Terminal organelle protein MG491 cause major motility and morphologic alterations on Mycoplasma genitalium.

Martinelli L, García-Morales L, Querol E, Piñol J, Fita I, Calisto BM.

PLoS Pathog. 12(4):e1005533. (2016)


Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis

de Cima S, Polo LM, Díez-Fernández C, Martínez AI, Cervera J, Fita I, Rubio V.

Sci. Rep. 5, 1695. (2015)


Selective photoregulation of the activity of glycogen synthase and glycogen phosphorylase, two key enzymes in glycogen metabolism.

Díaz-Lobo M, Garcia-Amorós J, Fita I, Velasco D, Guinovart JJ, Ferrer JC.

Org Biomol Chem. 13(26):7282-8. (2015)


Catalase-Peroxidase (KatG) structure and function.

I. Fita, X. Carpena, P. C. Loewen

In Heme Peroxidases, 133-155 (Royal Society of Chemistry Publishing). Ed. B. Dunford. (2015)


Catalase-Peroxidase: KatG.

Fita, I., Loewen, P. C. and Carpena, X.

Encyclopedia of Inorganic and Bioinorganic Chemistry. 1–14. (2015)


Eukaryotic Catalase-Peroxidase: The Role of the Trp-Tyr-Met Adduct in protein stability, substrate accessibility, and catalysis of Hydrogen Peroxide Dismutation.

Gasselhuber B, Carpena X, Graf MM, Pirker KF, Nicolussi A, Sündermann A, Hofbauer S, Zamocky M, Furtmüller PG, Jakopitsch C, Oostenbrink C, Fita I, Obinger C.

Biochemistry 54(35):5425-38. (2015)


Vibrational entropy of a protein: large differences between distinct conformations.

Goethe M, Fita I, Rubi JM.

J Chem Theory Comput 11(1):351-9.(2015)


Calcineurin undergoes a conformational switch evoked via peptidylprolyl isomerization.

A. Guasch, A. Aranguren-Ibáñez, R. Pérez-Luque, D. Aparicio, S. Martínez-Høyer, M. C. Mulero, E. Serrano-Candelas, M. Pérez-Riba ,I. Fita

PLos One, e0134569. (2015).


A major determinant for gliding motility in Mycoplasma genitalium: the interaction between the terminal organelle proteins MG200 and MG491.

L Martinelli, D Lalli, L Garćia-Morales, M Ratera, E Querol, J Piñol, I Fita, B. M. Calisto.

Journal of Biological Chemistry, M114. 594762 (2015)


An Ionizable Active-Site Tryptophan imparts Catalase Activity to a Peroxidase Core.

P. C. Loewen, X. Carpena, P. Vidossich, I. Fita, C. Rovira.

Journal of the American Chemical Society 136, 7249-52. (2014)


Binding of the anti-tubercular pro-drug isoniazid in the heme access channel of catalase–peroxidase (KatG). A combined structural and metadynamics investigation

P. Vidossich, P. C. Loewen, X. Carpena, G. Fiorin, I. Fita, C. Rovira

 J. Phys. Chem. B 20, 2924-31. (2014)


Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase.

Aparicio D, Pérez-Luque R, Carpena X, Díaz M, Ferrer JC, Loewen PC, Fita I

J Biol Chem 288: 11907-11919. (2013)


New features of vault architecture and dynamics revealed by novel refinement using the deformable elastic network approach.

Casañas A, Querol-Audí J, Guerra P, Pous J, Tanaka H, Tsukihara T, Verdaguer N, Fita I

Acta Crystallogr D Biol Crystallogr 69: 1054-1061. (2013)


Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa.

Garreta A, Val-Moraes SP, García-Fernández Q, Busquets M, Juan C, Oliver A, Ortiz A, Gaffney BJ, Fita I, Manresa A, Carpena X

FASEB J 27(12): 4811–4821 (2013)


Spectroscopic and Kinetic investigation of the reactions of Peroxyacetic Acid with Burkholderia pseudomallei Catalase-Peroxidase KatG.

Ivancich A, Donald LJ, Villanueva J, Wiseman B, Fita I, Loewen PC

Biochemistry 52: 7271-7282. (2013)


Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate.

Loewen PC, Didychuk AL, Switala J, Perez-Luque R, Fita I, Loewen MC

Acta Crystallogr Sect F Struct Biol Cryst Commun 69: 10-14. (2013)


X-ray crystallography of viruses.

Verdaguer N, Garriga D, Fita I

Subcell Biochem 68: 117-144. (2013)


Structure of glycerol-3-phosphate dehydrogenase (GPD1) from Saccharomyces cerevisiae at 2.45 Å resolution.

Alarcon DA, Nandi M, Carpena X, Fita I, Loewen PC

Acta Crystallogr Sect F Struct Biol Cryst Commun 68: 1279-1283. (2012)


The EAGR box structure: a motif involved in mycoplasma motility.

Calisto BM, Broto A, Martinelli L, Querol E, Piñol J, Fita I

Mol Microbiol 86: 382-393. (2012)


Vault particles: a new generation of delivery nanodevices.

Casañas A, Guerra P, Fita I, Verdaguer N

Curr Opin Biotechnol 23: 972-977. (2012)


Thirty years of heme catalases structural biology.

Díaz A, Loewen PC, Fita I, Carpena X

Arch Biochem Biophys 525: 102-110. (2012)


Thirty years of heme catalases structural biology.

Díaz A, Loewen PC, Fita I, Carpena X

Arch Biochem Biophys 525: 102-110. (2012)


Influence of main channel structure on H(2)O(2) access to the heme cavity of catalase KatE of Escherichia coli.

Jha V, Chelikani P, Carpena X, Fita I, Loewen PC

Arch Biochem Biophys 526: 54-59. (2012)


Crystal structure of Brucella abortus deoxyxylulose-5-phosphate reductoisomerase-like (DRL) enzyme involved in isoprenoid biosynthesis.

Pérez-Gil J, Calisto BM, Behrendt C, Kurz T, Fita I, Rodríguez-Concepción M

J Biol Chem 287: 15803-15809. (2012)


High conformational stability of secreted eukaryotic catalase-peroxidases: answers from first crystal structure and unfolding studies.

Zámocký M, García-Fernández Q, Gasselhuber B, Jakopitsch C, Furtmüller PG, Loewen PC, Fita I, Obinger C, Carpena X

J Biol Chem 287: 32254-32262. (2012)


Insight on an arginine synthesis metabolon from the tetrameric structure of yeast acetylglutamate kinase.

de Cima S, Gil-Ortiz F, Crabeel M, Fita I, Rubio V

PLoS One 7: e34734. (2011)


Re-engineering specificity in 1,3-1, 4-β-glucanase to accept branched xyloglucan substrates.

Addington T, Calisto B, Alfonso-Prieto M, Rovira C, Fita I, Planas A (2011)

Proteins 79: 365-375. (2011)


Processivity and subcellular localization of glycogen synthase depend on a non-catalytic high affinity glycogen-binding site.

Díaz A, Martínez-Pons C, Fita I, Ferrer JC, Guinovart JJ

J Biol Chem 286: 18505-18514. (2011)


Modulation of heme orientation and binding by a single residue in catalase HPII of Escherichia coli.

Jha V, Louis S, Chelikani P, Carpena X, Donald LJ, Fita I, Loewen PC (2011)

Biochemistry 50: 2101-2110. (2011)


Molecular basis of substrate-induced permeation by an amino acid antiporter.

Kowalczyk L, Ratera M, Paladino A, Bartoccioni P, Errasti-Murugarren E, Valencia E, Portella G, Bial S, Zorzano A, Fita I, Orozco M, Carpena X, Vázquez-Ibar JL, Palacín M

Proc Natl Acad Sci U S A 108: 3935-3940. (2011)


Two crystal structures of Escherichia coli N-acetyl-L-glutamate kinase demonstrate the cycling between open and closed conformations.

Gil-Ortiz F, Ramón-Maiques S, Fernández-Murga ML, Fita I, Rubio V

J Mol Biol 399: 476-490. (2010)


Substrate binding and catalysis in carbamate kinase ascertained by crystallographic and site-directed mutagenesis studies: movements and significance of a unique globular subdomain of this key enzyme for fermentative ATP production in bacteria.

Ramón-Maiques S, Marina A, Guinot A, Gil-Ortiz F, Uriarte M, Fita I, Rubio V

J Mol Biol 397: 1261-1275. (2010)


The dynamic role of distal side residues in heme hydroperoxidase catalysis. Interplay between X-ray crystallography and ab initio MD simulations.

Vidossich P, Alfonso-Prieto M, Carpena X, Fita I, Loewen PC, Rovira C

Arch Biochem Biophys 500: 37-44. (2010)


Isonicotinic acid hydrazide conversion to Isonicotinyl-NAD by catalase-peroxidases.

Wiseman B, Carpena X, Feliz M, Donald LJ, Pons M, Fita I, Loewen PC

J Biol Chem 285: 26662-26673. (2010)


Essential role of proximal histidine-asparagine interaction in mammalian peroxidases.

Carpena X, Vidossich P, Schroettner K, Calisto BM, Banerjee S, Stampler J, Soudi M, Furtmüller PG, Rovira C, Fita I, Obinger C

J Biol Chem 284: 25929-25937. (2009)


Structural and mechanistic insights into the association of PKCalpha-C2 domain to PtdIns(4,5)P2.

Guerrero-Valero M, Ferrer-Orta C, Querol-Audí J, Marin-Vicente C, Fita I, Gómez-Fernández JC, Verdaguer N, Corbalán-García S

Proc Natl Acad Sci U S A 106: 6603-6607. (2009)


Three-dimensional structure and enzymatic function of proapoptotic human p53-inducible quinone oxidoreductase PIG3.

Porté S, Valencia E, Yakovtseva EA, Borrás E, Shafqat N, Debreczeny JE, Pike ACW, Oppermann U, Farrés J, Fita I, Parés X

J Biol Chem 284: 17194-17205. (2009)


The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP.

Querol-Audí J, Casañas A, Usón I, Luque D, Castón JR, Fita I, Verdaguer N

EMBO J 28: 3450-3457. (2009)


Minor group human rhinovirus-receptor interactions: geometry of multimodular attachment and basis of recognition.

Querol-Audí J, Konecsni T, Pous J, Carugo O, Fita I, Verdaguer N, Blaas D

FEBS Lett 583: 235-240. (2009)


Aldo-keto reductases from the AKR1B subfamily: retinoid specificity and control of cellular retinoic acid levels.

Ruiz FX, Gallego O, Ardèvol A, Moro A, Domínguez M, Alvarez S, Alvarez R, de Lera AR, Rovira C, Fita I, Parés X, Farrés J

Chem Biol Interact 178: 171-177. (2009)


Electronic state of the molecular oxygen released by catalase.

Alfonso-Prieto M, Vidossich P, Rodríguez-Fortea A, Carpena X, Fita I, Loewen PC, Rovira C

J Phys Chem A 112: 12842-12848. (2008)


Structural and biochemical studies of TREX1 inhibition by metals. Identification of a new active histidine conserved in DEDDh exonucleases.

Brucet M, Querol-Audí J, Bertlik K, Lloberas J, Fita I, Celada A

Protein Sci 17: 2059-2069. (2008)


Arginine and nitrogen storage.

Llàcer JL, Fita I, Rubio V

Curr Opin Struct Biol 18: 673-681. (2008)


The structures and electronic configuration of compound I intermediates of Helicobacter pylori and Penicillium vitale catalases determined by X-ray crystallography and QM/MM density functional theory calculations.

Alfonso-Prieto M, Borovik A, Carpena X, Murshudov G, Melik-Adamyan W, Fita I, Rovira C, Loewen PC

J Am Chem Soc 129: 4193-4205. (2007)


Structure of the dimeric exonuclease TREX1 in complex with DNA displays a proline-rich binding site for WW Domains.

Brucet M, Querol-Audí J, Serra M, Ramirez-Espain X, Bertlik K, Ruiz L, Lloberas J, Macias MJ, Fita I, Celada A

J Biol Chem 282: 14547-14557. (2007)


Biosynthesis of isoprenoids in plants: structure of the 2C-methyl-D-erithrytol 2,4-cyclodiphosphate synthase from Arabidopsis thaliana. Comparison with the bacterial enzymes.

Calisto BM, Perez-Gil J, Bergua M, Querol-Audi J, Fita I, Imperial S

Protein Sci 16: 2082-2088. (2007)


Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei.

Deemagarn T, Wiseman B, Carpena X, Ivancich A, Fita I, Loewen PC

Proteins 66: 219-228. (2007)


The structure of human 4F2hc ectodomain provides a model for homodimerization and electrostatic interaction with plasma membrane.

Fort J, de la Ballina LR, Burghardt HE, Ferrer-Costa C, Turnay J, Ferrer-Orta C, Usón I, Zorzano A, Fernández-Recio J, Orozco M, Lizarbe MA, Fita I, Palacín M

J Biol Chem 282: 31444-31452. (2007)


Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10.

Gallego O, Ruiz FX, Ardèvol A, Domínguez M, Alvarez R, de Lera AR, Rovira C, Farrés J, Fita I, Parés X

Proc Natl Acad Sci U S A 104: 20764-20769. (2007)


The crystal structure of the complex of PII and acetylglutamate kinase reveals how PII controls the storage of nitrogen as arginine.

Llàcer JL, Contreras A, Forchhammer K, Marco-Marín C, Gil-Ortiz F, Maldonado R, Fita I, Rubio V

Proc Natl Acad Sci U S A 104: 17644-17649. (2007)


A novel two-domain architecture within the amino acid kinase enzyme family revealed by the crystal structure of Escherichia coli glutamate 5-kinase.

Marco-Marín C, Gil-Ortiz F, Pérez-Arellano I, Cervera J, Fita I, Rubio V

J Mol Biol 367: 1431-1446. (2007)


Versatility of the electronic structure of compound I in catalase-peroxidases.

Vidossich P, Alfonso-Prieto M, Carpena X, Loewen PC, Fita I, Rovira C

J Am Chem Soc 129: 13436-13446. (2007)


Roles for Arg426 and Trp111 in the modulation of NADH oxidase activity of the catalase-peroxidase KatG from Burkholderia pseudomallei inferred from pH-induced structural changes.

Carpena X, Wiseman B, Deemagarn T, Herguedas B, Ivancich A, Singh R, Loewen PC, Fita I

Biochemistry 45: 5171-5179. (2006)


Crystal structure of an archaeal glycogen synthase: insights into oligomerization and substrate binding of eukaryotic glycogen synthases

Horcajada C, Guinovart JJ, Fita I, Ferrer JC

J Biol Chem 281: 2923-2931. (2006).


Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa.

Ramón-Maiques S, Fernández-Murga ML, Gil-Ortiz F, Vagin A, Fita I, Rubio V

J Mol Biol 356: 695-713. (2006)


Combining experimental data for structure determination of flexible multimeric macromolecules by molecular replacement.

Trapani S, Abergel C, Gutsche I, Horcajada C, Fita I, Navaza J

Acta Crystallogr D Biol Crystallogr 62: 467-475. (2006)


Crystal structure of a putative type I restriction-modification S subunit from Mycoplasma genitalium.

Calisto BM, Pich OQ, Piñol J, Fita I, Querol E, Carpena X

J Mol Biol 351: 749-762. (2005)


A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases.

Carpena X, Wiseman B, Deemagarn T, Singh R, Switala J, Ivancich A, Fita I, Loewen PC

EMBO Rep 6: 1156-1162. (2005)


Characterization of a large subunit catalase truncated by proteolytic cleavage.

Chelikani P, Carpena X, Perez-Luque R, Donald LJ, Duckworth HW, Switala J, Fita I, Loewen PC

Biochemistry 44: 5597-5605. (2005)


Structural characterization of the Ser324Thr variant of the catalase-peroxidase (KatG) from Burkholderia pseudomallei.

Deemagarn T, Carpena X, Singh R, Wiseman B, Fita I, Loewen PC

J Mol Biol 345: 21-28. (2005)


Preliminary analysis of two and three dimensional crystals of vault ribonucleoprotein particles.

Querol-Audí J, Perez-Luque R, Fita I, Lopez-Iglesias C, Castón JR, Carrascosa JL, Verdaguer N

J Struct Biol 151: 111-115. (2005)


Structure of the C-terminal domain of the catalase-peroxidase KatG from Escherichia coli.

Carpena X, Melik-Adamyan W, Loewen PC, Fita I

Acta Crystallogr F 60: 1824-1832. (2004)


Diversity of structures and properties among catalases.

Chelikani P, Fita I, Loewen PC

Cell Mol Life Sci 61: 192-208. (2004)


Structure of Helicobacter pylori catalase, with and without formic acid bound, at 1.6 A resolution.

Loewen PC, Carpena X, Rovira C, Ivancich A, Perez-Luque R, Haas R, Odenbreit S, Nicholls P, Fita I

Biochemistry 43: 3089-3103. (2004)


Catalase-peroxidases (KatG) exhibit NADH oxidase activity.

Singh R, Wiseman B, Deemagarn T, Donald LJ, Duckworth HW, Carpena X, Fita I, Loewen PC

J Biol Chem 279: 43098-43106. (2004)


Apo and Holo structures of an NADPH-dependent cinnamyl alcohol dehydrogenase from Saccharomyces cerevisiae.

Valencia E, Larroy C, Ochoa WF, Parés X, Fita I, Biosca JA

J Mol Biol 341: 1049-1062. (2004)


X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein.

Verdaguer N, Fita I, Reithmayer M, Moser R, Blaas D

Nat Struct Mol Biol 11: 429-434. (2004)


Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A resolution.

Carpena X, Loprasert S, Mongkolsuk S, Switala J, Loewen PC, Fita I

J Mol Biol 327: 475-489. (2003)


Structure of the Clade 1 catalase, CatF of Pseudomonas syringae, at 1.8 A resolution

Carpena X, Soriano M, Klotz MG, Duckworth HW, Donald LJ, Melik-Adamyan W, Fita I, Loewen PC

Proteins 50: 423-436. (2003)


An electrical potential in the access channel of catalases enhances catalysis.

Chelikani P, Carpena X, Fita I, Loewen PC

J Biol Chem 278: 31290-31296. (2003)


Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry.

Donald LJ, Krokhin OV, Duckworth HW, Wiseman B, Deemagarn T, Singh R, Switala J, Carpena X, Fita I, Loewen PC

J Biol Chem 278: 35687-35692. (2003)


The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF(4)(-) transition state mimic.

Gil-Ortiz F, Ramón-Maiques S, Fita I, Rubio V

J Mol Biol 331: 231-244. (2003)


Crystallization and preliminary X-ray analysis of swine vesicular disease virus (SVDV).

Jimenez-Clavero MA, Ley V, Fita I, Verdaguer N

Acta Crystallogr D Biol Crystallogr 59: 541-543. (2003)


Retinoic acid binds to the C2-domain of protein kinase C(alpha).

Ochoa WF, Torrecillas A, Fita I, Verdaguer N, Corbalán-García S, Gomez-Fernandez JC

Biochemistry 42: 8774-8779. (2003)


Complete reversal of coenzyme specificity by concerted mutation of three consecutive residues in alcohol dehydrogenase.

Rosell A, Valencia E, Ochoa WF, Fita I, Parés X, Farrés J

J Biol Chem 278: 40573-40580. (2003)


Crystal structure of the vertebrate NADP(H)-dependent alcohol dehydrogenase (ADH8).

Rosell A, Valencia E, Parés X, Fita I, Farrés J, Ochoa WF

J Mol Biol 330: 75-85. (2003)


Crystallization and preliminary X-ray analysis of NADP(H)-dependent alcohol dehydrogenases from Saccharomyces cerevisiae and Rana perezi.

Valencia E, Rosell A, Larroy C, Farrés J, Biosca JA, Fita I, Parés X, Ochoa WF

Acta Crystallogr D Biol Crystallogr 59: 334-337. (2003)


Structure of swine vesicular disease virus: mapping of changes occurring during adaptation of human coxsackie B5 virus to infect swine.

Verdaguer N, Jimenez-Clavero MA, Fita I, Ley V

J Virol 77: 9780-9789. (2003)


Crystallization and preliminary X-ray analysis of the hydroperoxidase I C-terminal domain from Escherichia coli.

Carpena X, Guarné A, Ferrer JC, Alzari PM, Fita I, Loewen PC

Acta Crystallogr D Biol Crystallogr 58: 853-855. (2002)


Crystallization and preliminary X-ray analysis of the catalase-peroxidase KatG from Burkholderia pseudomallei.

Carpena X, Switala J, Loprasert S, Mongkolsuk S, Fita I, Loewen PC

Acta Crystallogr D Biol Crystallogr 58: 2184-2186. (2002)


Towards structural understanding of feedback control of arginine biosynthesis: cloning and expression of the gene for the arginine-inhibited N-acetyl-L-glutamate kinase from Pseudomonas aeruginosa, purification and crystallization of the recombinant enzyme and preliminary X-ray studies.

Fernández-Murga ML, Ramón-Maiques S, Gil-Ortiz F, Fita I, Rubio V

Acta Crystallogr D Biol Crystallogr 58: 1045-1047. (2002)


A crystallographic glimpse of a nucleotide triphosphate (AMPPNP) bound to a protein surface: external and internal AMPPNP molecules in crystalline N-acetyl-L-glutamate kinase.

Gil-Ortiz F, Fita I, Ramón-Maiques S, Marina A, Rubio V

Acta Crystallogr D Biol Crystallogr 58: 1892-1895. (2002)


Additional binding sites for anionic phospholipids and calcium ions in the crystal structures of complexes of the C2 domain of protein kinase calpha.

Ochoa WF, Corbalán-Garcia S, Eritja R, Rodríguez-Alfaro JA, Gómez-Fernández JC, Fita I, Verdaguer N

J Mol Biol 320: 277-291. (2002)


Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis.

Ramón-Maiques S, Marina A, Gil-Ortiz F, Fita I, Rubio V

Structure 10: 329-342. (2002)


Crystallization and preliminary X-ray analysis of clade I catalases from Pseudomonas syringae and Listeria seeligeri.

Carpena X, Perez R, Ochoa WF, Verdaguer N, Klotz MG, Switala J, Melik-Adamyan W, Fita I, Loewen PC

Acta Crystallogr D Biol Crystallogr 57: 1184-1186. (2001)


Theoretical study of the mechanisms of substrate recognition by catalase.

Kalko SG, Gelpí JL, Fita I, Orozco M

J Am Chem Soc 123: 9665-9672. (2001)


Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli.

Melik-Adamyan W, Bravo J, Carpena X, Switala J, Maté MJ, Fita I, Loewen PC

Proteins 44: 270-281. (2001)


Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains.

Ochoa WF, Garcia-Garcia J, Fita I, Corbalan-Garcia S, Verdaguer N, Gomez-Fernandez JC

J Mol Biol 311: 837-849. (2001)


Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes.

Guarné A, Hampoelz B, Glaser W, Carpena X, Tormo J, Fita I, Skern T

J Mol Biol 302: 1227-1240. (2000)


The need for a shared database infrastructure: combining X-ray crystallography and electron microscopy.

Kalko SG, Chagoyen M, Jiménez-Lozano N, Verdaguer N, Fita I, Carazo JM

Eur Biophys J 29: 457-462. (2000)


A multiply substituted G-H loop from foot-and-mouth disease virus in complex with a neutralizing antibody: a role for water molecules.

Ochoa WF, Kalko SG, Mateu MG, Gomes P, Andreu D, Domingo E, Fita I, Verdaguer N

J Gen Virol 81: 1495-1505. (2000)


The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases.

Ramón-Maiques S, Marina A, Uriarte M, Fita I, Rubio V

J Mol Biol 299: 463-476. (2000)


Structure of human rhinovirus serotype 2 (HRV2).

Verdaguer N, Blaas D, Fita I

J Mol Biol 300: 1179-1194. (2000)


Structure of catalase HPII from Escherichia coli at 1.9 A resolution.

Bravo J, Mate MJ, Schneider T, Switala J, Wilson K, Loewen PC, Fita I

Proteins 34: 155-166. (1999)


Organising multi-dimensional biological image information: the BioImage Database.

Carazo JM, Stelzer EH, Engel A, Fita I, Henn C, Machtynger J, McNeil P, Shotton DM, Chagoyen M, de Alarcón PA, Fritsch R, Heymann JB, Kalko S, Pittet JJ, Rodriguez-Tomé P, Boudier T

Nucleic Acids Res 27: 280-283. (1999)


Biochemical and structural studies with neutralizing antibodies raised against foot-and-mouth disease virus.

Domingo E, Verdaguer N, Ochoa WF, Ruiz-Jarabo CM, Sevilla N, Baranowski E, Mateu MG, Fita I

Virus Res 62: 169-175. (1999)


N-Acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms.

Gil F, Ramón-Maiques S, Marina A, Fita I, Rubio V

Acta Crystallogr D Biol Crystallogr 55: 1350-1352. (1999)


Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine.

Marina A, Alzari PM, Bravo J, Uriarte M, Barcelona B, Fita I, Rubio V

Protein Sci 8: 934-940. (1999)


Crystallization and preliminary structural results of catalase from human erythrocytes.

Maté MJ, Ortiz-Lombardía M, Marina A, Fita I

Acta Crystallogr D Biol Crystallogr 55: 1066-1068. (1999)


Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli.

Maté MJ, Sevinc MS, Hu B, Bujons J, Bravo J, Switala J, Ens W, Loewen PC, Fita I

J Biol Chem 274: 27717-27725. (1999)


Structure of catalase-A from Saccharomyces cerevisiae.

Maté MJ, Zamocky M, Nykyri LM, Herzog C, Alzari PM, Betzel C, Koller F, Fita I

J Mol Biol 286: 135-149. (1999)


The structures of picornaviral proteinases.

Seipelt J, Guarné A, Bergmann E, James M, Sommergruber W, Fita I, Skern T

Virus Res 62: 159-168. (1999)


Role of the lateral channel in catalase HPII of Escherichia coli.

Sevinc MS, Maté MJ, Switala J, Fita I, Loewen PC

Protein Sci 8: 490-498. (1999)


The carbamoyl-phosphate synthetase of Pyrococcus furiosus is enzymologically and structurally a carbamate kinase.

Uriarte M, Marina A, Ramón-Maiques S, Fita I, Rubio V

J Biol Chem 274: 16295-16303. (1999)


Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine.

Verdaguer N, Corbalan-Garcia S, Ochoa WF, Fita I, Gómez-Fernández JC

EMBO J 18: 6329-6338. (1999)


Crystallization and preliminary X-ray analysis of human rhinovirus serotype 2 (HRV2).

Verdaguer N, Marlovits TC, Bravo J, Stuart DI, Blaas D, Fita I

Acta Crystallogr D Biol Crystallogr 55: 1459-1461. (1999)


Flexibility of the major antigenic loop of foot-and-mouth disease virus bound to a Fab fragment of a neutralising antibody: structure and neutralisation.

Verdaguer N, Schoehn G, Ochoa WF, Fita I, Brookes S, King A, Domingo E, Mateu MG, Stuart D, Hewat EA

Virology 255: 260-268. (1999)


Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition.

Guarné A, Tormo J, Kirchweger R, Pfistermueller D, Fita I, Skern T

EMBO J 17: 7469-7479. (1998)


Solution conformation of an immunogenic peptide from HRV2: comparison with the conformation found in a complex with a Fab fragment of an anti-HRV2 neutralizing antibody.

Molins MA, Contreras MA, Fita I, Pons M

J Pept Sci 4: 101-110. (1998)


Truncation and heme pocket mutations reduce production of functional catalase HPII in Escherichia coli.

Sevinc MS, Switala J, Bravo J, Fita I, Loewen PC

Protein Eng 11: 549-555. (1998)


A structural model of picornavirus leader proteinases based on papain and bleomycin hydrolase.

Skern T, Fita I, Guarné A

J Gen Virol 79 (Pt 2): 301-307. (1998)


A similar pattern of interaction for different antibodies with a major antigenic site of foot-and-mouth disease virus: implications for intratypic antigenic variation.

Verdaguer N, Sevilla N, Valero ML, Stuart D, Brocchi E, Andreu D, Giralt E, Domingo E, Mateu MG, Fita I

J Virol 72: 739-748. (1998)


Crystallization and preliminary structural analysis of catalase A from Saccharomyces cerevisiae.

Berthet S, Nykyri LM, Bravo J, Mate MJ, Berthet-Colominas C, Alzari PM, Koller F, Fita I

Protein Sci 6: 481-483. (1997)


Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli.

Bravo J, Fita I, Ferrer JC, Ens W, Hillar A, Switala J, Loewen PC

Protein Sci 6: 1016-1023. (1997)


Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop.

Hewat EA, Verdaguer N, Fita I, Blakemore W, Brookes S, King A, Newman J, Domingo E, Mateu MG, Stuart DI

EMBO J 16: 1492-1500. (1997)


The structure of alfalfa mosaic virus capsid protein assembled as a T=1 icosahedral particle at 4.0-A resolution.

Kumar A, Reddy VS, Yusibov V, Chipman PR, Hata Y, Fita I, Fukuyama K, Rossmann MG, Loesch-Fries LS, Baker TS, Johnson JE

J Virol 71: 7911-7916. (1997)


Efficient neutralization of foot-and-mouth disease virus by monovalent antibody binding.

Verdaguer N, Fita I, Domingo E, Mateu MG

J Virol 71: 9813-9816. (1997)


Conformation of the hypervariable region L3 without the key proline residue.

Guarné A, Bravo J, Calvo J, Lozano F, Vives J, Fita I

Protein Sci 5: 167-169. (1996)


Crystallization and preliminary X-ray diffraction studies of the Lb proteinase from foot-and-mouth disease virus.

Guarné A, Kirchweger R, Verdaguer N, Liebig HD, Blaas D, Skern T, Fita I

Protein Sci 5: 1931-1933. (1996)


Structure of the heme d of Penicillium vitale and Escherichia coli catalases.

Murshudov GN, Grebenko AI, Barynin V, Dauter Z, Wilson KS, Vainshtein BK, Melik-Adamyan W, Bravo J, Ferrán JM, Ferrer JC, Switala J, Loewen PC, Fita I

J Biol Chem 271: 8863-8868. (1996)


Induced pocket to accommodate the cell attachment Arg-Gly-Asp motif in a neutralizing antibody against foot-and-mouth-disease virus.

Verdaguer N, Mateu MG, Bravo J, Domingo E, Fita I

J Mol Biol 256: 364-376. (1996)


Crystal structure of catalase HPII from Escherichia coli.

Bravo J, Verdaguer N, Tormo J, Betzel C, Switala J, Loewen PC, Fita I

Structure 3: 491-502. (1995)


Molecular evolution of aphthoviruses.

Domingo E, Mateu MG, Escarmís C, Martínez-Salas E, Andreu D, Giralt E, Verdaguer N, Fita I

Virus Genes 11: 197-207. (1995)


Determination of hemihedral twinning and initial structural analysis of crystals of the procarboxypeptidase A ternary complex.

Gomis-Rüth FX, Fita I, Kiefersauer R, Huber R, Avilés FX, Navaza J

Acta Crystallogr D Biol Crystallogr 51: 819-823. (1995)


Crystallization, characterization, and preliminary crystallographic studies of mitochondrial carbamoyl phosphate synthetase I of Rana catesbeiana.

Marina A, Bravo J, Fita I, Rubio V

Proteins 22: 193-196. (1995)


Docking of a human rhinovirus neutralizing antibody onto the viral capsid.

Tormo J, Centeno NB, Fontana E, Bubendorfer T, Fita I, Blaas D

Proteins 23: 491-501. (1995)


Cyclic peptides as conformationally restricted models of viral antigens: application to foot-and-mouth disease virus.

Valero ML, Camarero JA, Adeva A, Verdaguer N, Fita I, Mateu MG, Domingo E, Giralt E, Andreu D

Biomed Pept Proteins Nucleic Acids 1: 133-140. (1995)


Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: direct involvement of the Arg-Gly-Asp motif in the interaction.

Verdaguer N, Mateu MG, Andreu D, Giralt E, Domingo E, Fita I

EMBO J 14: 1690-1696. (1995)


Investigation of shape variations in the antibody binding site by molecular dynamics computer simulation.

de la Cruz X, Mark AE, Tormo J, Fita I, van Gunsteren WF

J Mol Biol 236: 1186-1195. (1994)


Structure of ribonuclease A derivative II at 2.1-A resolution.

Boqué L, Gràcia Coll M, Vilanova M, Cuchillo CM, Fita I

J Biol Chem 269: 19707-19712. (1994)


Crystallization, characterization and preliminary crystallographic studies of carbamate kinase of Streptococcus faecium.

Marina A, Bravo J, Fita I, Rubio V

J Mol Biol 235: 1345-1347. (1994)


Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2.

Tormo J, Blaas D, Parry NR, Rowlands D, Stuart D, Fita I

EMBO J 13: 2247-2256. (1994)


Crystallization and preliminary X-ray diffraction studies of a monoclonal antibody Fab fragment against foot-and-mouth disease virus and of its complex with the main antigenic site peptide.

Verdaguer N, Mateu MG, Bravo J, Tormo J, Giralt E, Andreu D, Domingo E, Fita I

Proteins 18: 201-203. (1994)


Molecular structure of the A-tract DNA dodecamer d(CGCAAATTTGCG) complexed with the minor groove binding drug netropsin.

Tabernero L, Verdaguer N, Coll M, Fita I, van der Marel GA, van Boom JH, Rich A, Aymamí J

Biochemistry 32: 8403-8410. (1993)


Representation of noncovalent interactions in protein structures.

de la Cruz X, Reverter J, Fita I

J Mol Graph 10: 96-100, 110. (1992)


Crystal structure of a helical oligopeptide model of polyglycine II and of other polyamides: acetyl-(glycyl-beta-alanyl)2-NH propyl.

Tormo J, Puiggali J, Vives J, Fita I, Lloveras J, Bella J, Aymamí J, Subirana JA

Biopolymers 32: 643-648. (1992)


Three-dimensional structure of the Fab fragment of a neutralizing antibody to human rhinovirus serotype 2.

Tormo J, Stadler E, Skern T, Auer H, Kanzler O, Betzel C, Blaas D, Fita I

Protein Sci 1: 1154-1161. (1992)


Molecular structure of a complete turn of A-DNA.

Verdaguer N, Aymami J, Fernández-Forner D, Fita I, Coll M, Huynh-Dinh T, Igolen J, Subirana JA

J Mol Biol 221: 623-635. (1991)


Crystallization and preliminary x-ray diffraction studies of the Fab fragment of a neutralizing monoclonal antibody directed against human rhinovirus serotype 2.

Tormo J, Fita I, Kanzler O, Blaas D

J Biol Chem 265: 16799-16800. (1990)


Crystallization and preliminary X-ray diffraction analysis of catalase HPII from Escherichia coli.

Tormo J, Fita I, Switala J, Loewen PC

J Mol Biol 213: 219-220. (1990)


Molecular structure of L-lysyl-L-tyrosyl-L-serine acetate.

Verdaguer N, Fita I, Subirana JA

Int J Biol Macromol 12: 315-320. (1990)


Conformations in crystals and solutions of d(CACGTG), d(CCGCGG) and d(GGCGCC) studied by vibrational spectroscopy.

Urpi L, Ridoux JP, Liquier J, Verdaguer N, Fita I, Subirana JA, Iglesias F, Huynh-Dinh T, Igolen J, Taillandier E

Nucleic Acids Res 17: 6669-6680. (1989)


Structure of d(CACGTG), a Z-DNA hexamer containing AT base pairs.

Coll M, Fita I, Lloveras J, Subirana JA, Bardella F, Huynh-Dinh T, Igolen J

Nucleic Acids Res 16: 8695-8705. (1988)


Molecular structure of L-lysyl-L-alanyl-L-alanine: a tripeptide found in histone H1.

Verdaguer N, Urpí L, Fita I, Subirana JA

Biopolymers 27: 1887-1896. (1988)


Comparison of beef liver and Penicillium vitale catalases.

Melik-Adamyan WR, Barynin VV, Vagin AA, Borisov VV, Vainshtein BK, Fita I, Murthy MR, Rossmann MG

J Mol Biol 188: 63-72. (1986)


Modelling and refinement of the crystal structure of nucleoprotamine from Gibbula divaricata.

Puigjaner LC, Fita I, Arnott S, Chandrasekaran R, Subirana JA

J Biomol Struct Dyn 3: 1067-1078. (1986)


Three-dimensional structure of catalase from Penicillium vitale at 2.0 A resolution.

Vainshtein BK, Melik-Adamyan WR, Barynin VV, Vagin AA, Grebenko AI, Borisov VV, Bartels KS, Fita I, Rossmann MG

J Mol Biol 188: 49-61. (1986)


The structure of a T = 1 icosahedral empty particle from southern bean mosaic virus.

Erickson JW, Silva AM, Murthy MR, Fita I, Rossmann MG

Science 229: 625-629. (1985)


The active center of catalase.

Fita I, Rossmann MG

J Mol Biol 185: 21-37. (1985)


The NADPH binding site on beef liver catalase.

Fita I, Rossmann MG

Proc Natl Acad Sci U S A 82: 1604-1608. (1985)


X-ray diffraction study of DNA complexes with arginine peptides and their relation to nucleoprotamine structure.

Fita I, Campos JL, Puigjaner LC, Subirana JA

J Mol Biol 167: 157-177. (1983)


The subunit structure of chromatin fibres.

Subirana JA, Muñoz-Guerra S, Martínez AB, Pérez-Grau L, Marcet X, Fita I

Chromosoma 83: 455-471. (1981)


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