1l6p
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jpe|1JPE]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l6p OCA], [http://www.ebi.ac.uk/pdbsum/1l6p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l6p RCSB]</span> | ||
}} | }} | ||
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[[Category: immunoglobulin-like fold]] | [[Category: immunoglobulin-like fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:58:53 2008'' |
Revision as of 18:58, 30 March 2008
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| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Related: | 1JPE
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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