3bqh
From Proteopedia
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'''Structure of the central domain (MsrA) of Neisseria meningitidis PilB (oxidized form)''' | '''Structure of the central domain (MsrA) of Neisseria meningitidis PilB (oxidized form)''' | ||
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A Structural Analysis of the Catalytic Mechanism of Methionine Sulfoxide Reductase A from Neisseria meningitidis., Ranaivoson FM, Antoine M, Kauffmann B, Boschi-Muller S, Aubry A, Branlant G, Favier F, J Mol Biol. 2008 Jan 16;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18255097 18255097] | A Structural Analysis of the Catalytic Mechanism of Methionine Sulfoxide Reductase A from Neisseria meningitidis., Ranaivoson FM, Antoine M, Kauffmann B, Boschi-Muller S, Aubry A, Branlant G, Favier F, J Mol Biol. 2008 Jan 16;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18255097 18255097] | ||
[[Category: Neisseria meningitidis serogroup a]] | [[Category: Neisseria meningitidis serogroup a]] | ||
| - | [[Category: Peptide-methionine-(S)-S-oxide reductase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Favier, F.]] | [[Category: Favier, F.]] | ||
[[Category: Kauffmann, B.]] | [[Category: Kauffmann, B.]] | ||
[[Category: Ranaivoson, F M.]] | [[Category: Ranaivoson, F M.]] | ||
| - | [[Category: | + | [[Category: Electron transport]] |
| - | [[Category: | + | [[Category: Methionine sulfoxide reductase some]] |
| - | [[Category: | + | [[Category: Multifunctional enzyme]] |
| - | [[Category: | + | [[Category: Oxidized form]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Pilb]] |
| - | [[Category: | + | [[Category: Redox-active center]] |
| - | [[Category: | + | [[Category: Transport]] |
| - | [[Category: | + | [[Category: X-ray structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:00:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:00, 4 May 2008
Structure of the central domain (MsrA) of Neisseria meningitidis PilB (oxidized form)
Overview
The methionine sulfoxide reductases (Msrs) are thioredoxin-dependent oxidoreductases that catalyse the reduction of the sulfoxide function of the oxidized methionine residues. These enzymes have been shown to regulate the life span of a wide range of microbial and animal species and to play the role of physiological virulence determinant of some bacterial pathogens. Two structurally unrelated classes of Msrs exist, MsrA and MsrB, with opposite stereoselectivity towards the R and S isomers of the sulfoxide function, respectively. Both Msrs share a similar three-step chemical mechanism including (1) the formation of a sulfenic acid intermediate on the catalytic Cys with the concomitant release of the product-methionine, (2) the formation of an intramonomeric disulfide bridge between the catalytic and the regenerating Cys and (3) the reduction of the disulfide bridge by thioredoxin or its homologues. In this study, four structures of the MsrA domain of the PilB protein from Neisseria meningitidis, representative of four catalytic intermediates of the MsrA catalytic cycle, were determined by X-ray crystallography: the free reduced form, the Michaelis-like complex, the sulfenic acid intermediate and the disulfide oxidized forms. They reveal a conserved overall structure up to the formation of the sulfenic acid intermediate, while a large conformational switch is observed in the oxidized form. The results are discussed in relation to those proposed from enzymatic, NMR and theoretical chemistry studies. In particular, the substrate specificity and binding, the catalytic scenario of the reductase step and the relevance and role of the large conformational change observed in the oxidized form are discussed.
About this Structure
3BQH is a Single protein structure of sequence from Neisseria meningitidis serogroup a. Full crystallographic information is available from OCA.
Reference
A Structural Analysis of the Catalytic Mechanism of Methionine Sulfoxide Reductase A from Neisseria meningitidis., Ranaivoson FM, Antoine M, Kauffmann B, Boschi-Muller S, Aubry A, Branlant G, Favier F, J Mol Biol. 2008 Jan 16;. PMID:18255097 Page seeded by OCA on Sun May 4 21:00:57 2008
