4pq1

Crystal structure and functional implications of a DsbF homologue from Corynebacterium diphtheriae

spinqualitylabelsall models 4pq1, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pq1 is a 2 chain structure with sequence from Corynebacterium diphtheriae NCTC 13129. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.097Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6NJJ0_CORDI Publication Abstract from PubMed Disulfide-bond formation, mediated by the Dsb family of proteins, is important in the correct folding of secreted or extracellular proteins in bacteria. In Gram-negative bacteria, disulfide bonds are introduced into the folding proteins in the periplasm by DsbA. DsbE from Escherichia coli has been implicated in the reduction of disulfide bonds in the maturation of cytochrome c. The Gram-positive bacterium Mycobacterium tuberculosis encodes DsbE and its homologue DsbF, the structures of which have been determined. However, the two mycobacterial proteins are able to oxidatively fold a protein in vitro, unlike DsbE from E. coli. In this study, the crystal structure of a DsbE or DsbF homologue protein from Corynebacterium diphtheriae has been determined, which revealed a thioredoxin-like domain with a typical CXXC active site. Structural comparison with M. tuberculosis DsbF would help in understanding the function of the C. diphtheriae protein. Structure of a DsbF homologue from Corynebacterium diphtheriae.,Um SH, Kim JS, Lee K, Ha NC Acta Crystallogr F Struct Biol Commun. 2014 Sep;70(Pt 9):1167-72. doi:, 10.1107/S2053230X14016355. Epub 2014 Aug 29. PMID:25195886 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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