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Disulfide bond isomerization in prokaryotes.
Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109-1048, USA.
Proteins with multiple cysteine residues often require disulfide isomerization reactions before they attain their correct conformation. In prokaryotes this reaction is catalyzed mainly by DsbC, a protein that shares many similarities in structure and mechanism to the eukaryotic protein disulfide isomerase. This review discusses the current knowledge about disulfide isomerization in prokaryotes.
PMID: 18342631 [PubMed - indexed for MEDLINE]
PMCID: PMC2391271
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