1l1d
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Crystal structure of the C-terminal methionine sulfoxide reductase domain (MsrB) of N. gonorrhoeae pilB
OverviewOverview
Methionine sulfoxide reductases (Msr) protect against oxidative damage, that can contribute to cell death. The tandem Msr domains (MsrA and MsrB), of the pilB protein from Neisseria gonorrhoeae each reduce different, epimeric forms of methionine sulfoxide. The overall fold of the MsrB, domain revealed by the 1.85 A crystal structure shows no resemblance to, the previously determined MsrA structures from other organisms. Despite, the lack of homology, the active sites show approximate mirror symmetry., In each case, conserved amino acid motifs mediate the stereo-specific, recognition and reduction of the substrate. Unlike the MsrA domain, the, MsrB domain activates the cysteine or selenocysteine nucleophile through a, unique Cys-Arg-Asp/Glu catalytic triad. The collapse of the reaction, intermediate most likely results in the formation of a sulfenic or, selenenic acid moiety. Regeneration of the active site occurs through a, series of thiol-disulfide exchange steps involving another active site Cys, residue and thioredoxin. These observations have broad implications for, modular catalysis, antibiotic drug design and continuing longevity studies, in mammals.
About this StructureAbout this Structure
1L1D is a Single protein structure of sequence from Neisseria gonorrhoeae with CAC as ligand. Active as L-methionine-(S)-S-oxide reductase, with EC number 1.8.4.13 Full crystallographic information is available from OCA.
ReferenceReference
The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB., Lowther WT, Weissbach H, Etienne F, Brot N, Matthews BW, Nat Struct Biol. 2002 May;9(5):348-52. PMID:11938352
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