Exploring the catalytic mechanism of the first dimeric Bcp: Functional, structural and docking analyses of Bcp4 from Sulfolobus solfataricus(373 views) Limauro D, D'Ambrosio K, Langella E, De Simone G, Galdi I, Pedone C, Pedone E, Bartolucci S
Keywords: Bacterioferritin Comigratory Proteins, Disulfide Bond, Peroxiredoxin, Protein Disulfide Oxidoreductase, Sulfolobus Solfataricus, Bacterial Protein, Mutant Protein, Unclassified Drug, Article, Biocatalysis, Biochemistry, Comparative Study, Crystal Structure, Molecular Docking, Nonhuman, Protein Analysis, Protein Function, Protein Motif, Protein Protein Interaction, Protein Structure, Reaction Analysis, Site Directed Mutagenesis, Structure Analysis, X Ray Crystallography, Antioxidants, X-Ray, Mutation, Oxidation-Reduction, Protein Binding, Protein Multimerization,
Affiliations: *** IBB - CNR ***
Dipartimento di Biologia Strutturale e Funzionale, Universita degli Studi di Napoli ''Federico II'', Complesso Universitario Monte S. Angelo, Via Cinthia, 80126 Naples, Italy.
Istituto di Biostrutture e Bioimmagini-CNR, Via Mezzocannone 16, 80134 Naples, Italy
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Laskowsky, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M., PROCHECK: a program to check the stereochemical quality of protein structures (1993) J. Appl. Cryst., 26, pp. 283-329
Choi, H. J., Kang, S. W., Yang, C. H., Rhee, S. G., Ryu, S. E., Crystal structure of a novel human peroxidase enzyme at 2. 0 resolution (1998) Nat. Struct. Biol., 5, pp. 400-406
Declercq, J. P., Evrard, C., Clippe, A., Vander Stricht, D., Bernard, A., Knoops, B., Crystal structure of human peroxiredoxin 5, a novel type of Mammalian peroxiredoxin at 1. 5 resolution (2001) J. Mol. Biol., 311, pp. 751-759
Sarma, G. N., Nickel, C., Rahlfs, S., Fischer, M., Becker, K., Karplus, P. A., Crystal structure of a novel Plasmodium falciparum 1-Cys peroxiredoxin (2005) J. Mol. Biol., 346, pp. 1021-1034
Koh, C. S., Didierjean, C., Navrot, N., Panjikar, S., Mulliert, G., Rouhier, N., Jacquot, J. P., Corbier, C., Crystal structures of a poplar thioredoxin peroxidase that exhibits the structure of glutathione peroxidases: insights into redox-driven conformational changes (2007) J. Mol. Biol., 370, pp. 512-529
Exploring the catalytic mechanism of the first dimeric Bcp: Functional, structural and docking analyses of Bcp4 from Sulfolobus solfataricus
The detoxification from peroxides in Sulfolobus solfataricus is performed by the Bacterioferritin comigratory proteins (Bcps), Bcp1 (Sso2071), Bcp2 (Sso2121), Bcp3 (Sso2255) and Bcp4 (Sso2613), antioxidant enzymes belonging to one of the subfamilies of the Peroxiredoxins. In this paper we report on the functional, structural and docking analyses of Bcp4, characterized by the CXXXXC motif in the active site. Bcp4 represents the first dimeric Bcp so far investigated. Biochemical studies showed that the protein has a non-covalent dimeric structure and adopts an atypical 2-Cys catalytic mechanism. The X-ray structure of the double mutant C45S/C50S, representative of the fully reduced enzyme state, described the protein dimeric arrangement. Finally, concurrent availability of the crystallographic structure of the monomeric Bcp1 allowed comparative analysis of the interaction with Protein Disulfide Oxidoreductase SsPDO (Sso0192), involved in the reduction of both Bcp1 and Bcp4, through a protein-protein docking approach. Copyright 2010 Elsevier Masson SAS. All rights reserved.
Exploring the catalytic mechanism of the first dimeric Bcp: Functional, structural and docking analyses of Bcp4 from Sulfolobus solfataricus