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From Wikipedia, the free encyclopedia
Disulfide bond formation protein B (DsbB) is a protein component of the pathway that leads to disulfide bond formation in periplasmic proteins of Escherichia coli (P0A6M2) and other bacteria. In Bacillus subtilis it is known as BdbC (O32217).
![]() | This article may be too technical for most readers to understand. (June 2012) |
![]() Disulfide bond formation protein B (red), complex with DsbA (blue) | |||||||||
Identifiers | |||||||||
---|---|---|---|---|---|---|---|---|---|
Symbol | DsbB | ||||||||
Pfam | PF02600 | ||||||||
InterPro | IPR003752 | ||||||||
TCDB | 5.A.2 | ||||||||
OPM superfamily | 173 | ||||||||
OPM protein | 2hi7 | ||||||||
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The DsbB protein oxidizes the periplasmic protein DsbA which in turn oxidizes cysteines in other periplasmic proteins in order to make disulfide bonds.[1] DsbB acts as a redox potential transducer across the cytoplasmic membrane. It is a membrane protein which spans the membrane four times with both the N- and C-termini of the protein are in the cytoplasm. Each of the periplasmic domains of the protein has two essential cysteines. The two cysteines in the first periplasmic domain are in a Cys-X-Y-Cys configuration that is characteristic of the active site of other proteins involved in disulfide bond formation, including DsbA and protein disulfide isomerase.[2]
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