4PQ1

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

Summary for 4PQ1

• Entry DOI: 10.2210/pdb4pq1/pdb
• Descriptor: Putative electron transport related protein (2 entities in total)
• Functional Keywords: thioredoxin-like region, reductant, oxidant, oxidoreductase
• Biological source: Corynebacterium diphtheriae
• Total number of polymer chains: 2
• Total formula weight: 34614.58

Authors

Um, S.H.,Kim, J.S.,Yoon, B.Y.,Ha, N.C. (deposition date: 2014-02-28, release date: 2014-09-10, Last modification date: 2024-10-09)

Primary citation

Um, S.H.,Kim, J.S.,Lee, K.,Ha, N.C.
Structure of a DsbF homologue from Corynebacterium diphtheriae.
Acta Crystallogr.,Sect.F, 70:1167-1172, 2014

PubMed Abstract: 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.

PubMed: 25195886
DOI: 10.1107/S2053230X14016355

Experimental method

X-RAY DIFFRACTION (2.097 Å)