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PDBsum entry 1l6p
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Electron transport
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PDB id
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1l6p
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Thiol-Disulfide exchange in an immunoglobulin-Like fold: structure of the n-Terminal domain of dsbd.
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Authors
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C.W.Goulding,
M.R.Sawaya,
A.Parseghian,
V.Lim,
D.Eisenberg,
D.Missiakas.
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Ref.
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Biochemistry, 2002,
41,
6920-6927.
[DOI no: ]
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PubMed id
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Abstract
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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.
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