title: Disulfide bond isomerization in prokaryotes.
abstract: 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.
authors.affiliation: Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109-1048, USA.
authors.forename: Stefan
authors.initials: S
authors.lastname: Gleiter
authors.forename: James C A
authors.initials: JC
authors.lastname: Bardwell
mesh_terms: D000818:Animals; D004220:Disulfides / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D007536:Isomerism; D011387:Prokaryotic Cells / Q000201:enzymology*; D011487:Protein Conformation; D019704:Protein Disulfide-Isomerases / Q000737:chemistry* / Q000502:physiology
chemical_list: D004220:Disulfides; D019704:Protein Disulfide-Isomerases