1xdq

Structural and Biochemical Identification of a Novel Bacterial Oxidoreductase

spinqualitylabelsall models 1xdq, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1xdq is a 5 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.55Å Ligands: MO, MTE, O, URE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MSRP_ECOLI Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons (PubMed:26641313). Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine (PubMed:26641313). MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal (PubMed:26641313). The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide (PubMed:26641313). Can catalyze the reduction of a variety of substrates in vitro, including dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide (PubMed:15355966). Cannot reduce cyclic N-oxides (PubMed:15355966). Shows no activity as sulfite oxidase (PubMed:15355966). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also Sulfite Oxidase

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