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DsbC protein family : ウィキペディア英語版 | DsbC protein family
DsbC (Disulfide bond C) is a prokaryotic disulfide bond isomerase. The formation of native disulfide bonds play an important role in the proper folding of proteins and stabilize tertiary structures of the protein. DsbC is one of 6 proteins in the Dsb family in prokaryotes. The other proteins are DsbA, DsbB, DsbD, DsbE and DsbG. These enzymes work in tandem with each other to form disulfide bonds during the expression of proteins. DsbC and DsbG act as proofreaders of the disulfide bonds that are formed. They break non-native disulfide bonds that were formed and act as chaperones for the formation of native disulfide bonds. The isomerization of disulfide bonds occurs in the periplasm. ==Enzyme Mechanism==
DsbA, DsbC and DsbG have a common Cys-Xxx-Xxx-Cys (Cys-Cysteine) motif in their active site, where Xxx can be any any amino acid. In the periplasm, DsbA oxidizes thiols in cysteines to form disulfide bonds in proteins. DsbA receives it’s oxidizing potential from the cytosol through DsbB. However, the probability of forming a non-native disulfide bond increases with the number of cysteines in the protein sequence. This leads to improperly folded proteins. DsbC and DsbG facilitate the proper folding of the protein by breaking non-native disulfide bonds. In addition to this, DsbC also shows chaperone activity. The reduced cysteine on DsbC performs a nucleophilic attack on the target non-native disulfide bond, to form an unstable disulfide bond between DsbC and the protein. Another thiolate group in the protein then attacks this unstable bond. The final result would be the formation of a native disulfide bond and the reformation of the thiolate group in DsbC. DsbG also acts with a similar mechanism, but has a higher selectivity when compared with DsbC. Both DsbC and DsbG receive their reducing power, through DsbD, from the cytosol. DsbC and DsbG have be maintained in their reduced forms to ensure proper folding of proteins, with the formation of multiple disulfide bonds.
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