title: Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.
abstract: DsbC is one of five Escherichia coli proteins required for disulfide bond formation and is thought to function as a disulfide bond isomerase during oxidative protein folding in the periplasm. DsbC is a 2 x 23 kDa homodimer and has both protein disulfide isomerase and chaperone activity. We report the 1.9 A resolution crystal structure of oxidized DsbC where both Cys-X-X-Cys active sites form disulfide bonds. The molecule consists of separate thioredoxin-like domains joined via hinged linker helices to an N-terminal dimerization domain. The hinges allow relative movement of the active sites, and a broad uncharged cleft between them may be involved in peptide binding and DsbC foldase activities.
authors.affiliation: School of Biological Sciences, Auckland University, Private Bag 92019 Auckland New Zealand.
authors.forename: A A
authors.initials: AA
authors.lastname: McCarthy
authors.forename: P W
authors.initials: PW
authors.lastname: Haebel
authors.forename: A
authors.initials: A
authors.lastname: Törrönen
authors.forename: V
authors.initials: V
authors.lastname: Rybin
authors.forename: E N
authors.initials: EN
authors.lastname: Baker
authors.forename: P
authors.initials: P
authors.lastname: Metcalf
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D020134:Catalytic Domain; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D004220:Disulfides / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019704:Protein Disulfide-Isomerases / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012997:Solvents; D013879:Thioredoxins / Q000378:metabolism
chemical_list: D004220:Disulfides; D012997:Solvents; D013879:Thioredoxins; D019704:Protein Disulfide-Isomerases