3bqe

Structure of the central domain (MsrA) of Neisseria meningitidis PilB (reduced form)

spinqualitylabelsall models 3bqe, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3bqe is a 1 chain structure with sequence from Neima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3bqf, 3bqg, 3bqh Gene: pilB (NEIMA) Activity: Peptide-methionine (S)-S-oxide reductase, with EC number 1.8.4.11 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MSRAB_NEIMA] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 Mar 14;377(1):268-80. Epub 2008 Jan 16. PMID:18255097 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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