3cw0 | pdb_00003cw0
E.coli DmsD
Structural highlights
Function[DMSD_ECOLI] Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein.[1] [2] [3] [4] 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 PubMedThe translocation of folded proteins via the twin-arginine translocation (Tat) pathway is regulated to prevent the futile export of inactive substrate. DmsD is part of a class of cytoplasmic chaperones that play a role in preventing certain redox proteins from premature transport. DmsD from Escherichia coli has been crystallized in space group P4(1)2(1)2, with unit-cell parameters a = b = 97.45, c = 210.04 A, in the presence of a small peptide. The structure has been solved by molecular replacement to a resolution of 2.4 A and refined to an R factor of 19.4%. There are four molecules in the asymmetric unit that may mimic a higher order structure in vivo. There appears to be density for the peptide in a predicted binding pocket, which lends support to its role as the signal-recognition surface for this class of proteins. Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli.,Ramasamy SK, Clemons WM Jr Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Aug 1;65(Pt, 8):746-50. Epub 2009 Jul 21. PMID:19652330[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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