1l6p
From Proteopedia
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N-terminal of DsbD (residues 20-144) from E. coli.
Overview
Escherichia coli DsbD transports electrons across the plasma membrane, a, pathway that leads to the reduction of protein disulfide bonds. Three, secreted thioredoxin-like factors, DsbC, DsbE, and DsbG, reduce protein, disulfide bonds whereby an active site C-X-X-C motif is oxidized to, generate a disulfide bond. DsbD catalyzes the reduction of the disulfide, of DsbC, DsbE, and DsbG but not of the thioredoxin-like oxidant DsbA. The, reduction of DsbC, DsbE, and DsbG occurs by transport of electrons from, cytoplasmic thioredoxin to the C-terminal thioredoxin-like domain of DsbD, (DsbD(C)). The N-terminal domain of DsbD, DsbD(N), acts as a versatile, adaptor in electron transport and is capable of forming disulfides with, oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD(C). Isolated, DsbD(N) is functional in electron transport in vitro. Crystallized DsbD(N), assumes an immunoglobulin-like fold that encompasses two active site, cysteines, C103 and C109, forming a disulfide bond between beta-strands., The disulfide of DsbD(N) is shielded from the environment and capped by a, phenylalanine (F70). A model is discussed whereby the immunoglobulin fold, of DsbD(N) may provide for the discriminating interaction with, thioredoxin-like factors, thereby triggering movement of the phenylalanine, cap followed by disulfide rearrangement.
About this Structure
1L6P is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD., Goulding CW, Sawaya MR, Parseghian A, Lim V, Eisenberg D, Missiakas D, Biochemistry. 2002 Jun 4;41(22):6920-7. PMID:12033924
Page seeded by OCA on Tue Nov 20 20:19:15 2007
