1dsb: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsb OCA], [http://www.ebi.ac.uk/pdbsum/1dsb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dsb RCSB]</span> | |||
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[[Category: disulfide oxidoreductase]] | [[Category: disulfide oxidoreductase]] | ||
''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 19:47:43 2008'' | ||
Revision as of 19:47, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR DISULPHIDE BOND FORMATION IN VIVO
OverviewOverview
Proteins that contain disulphide bonds are often slow to fold in vitro because the oxidation and correct pairing of the cysteine residues is rate limiting. The folding of such proteins is greatly accelerated in Escherichia coli by DsbA, but the mechanism of this rate enhancement is not well understood. Here we report the crystal structure of oxidized DsbA and show that it resembles closely the ubiquitous redox protein thioredoxin, despite very low sequence similarity. An important difference, however, is the presence of another domain which forms a cap over the thioredoxin-like active site of DsbA. The redox-active disulphide bond, which is responsible for the oxidation of substrates, is thus at a domain interface and is surrounded by grooves and exposed hydrophobic side chains. These features suggest that DsbA might act by binding to partially folded polypeptide chains before oxidation of cysteine residues.
About this StructureAbout this Structure
1DSB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the DsbA protein required for disulphide bond formation in vivo., Martin JL, Bardwell JC, Kuriyan J, Nature. 1993 Sep 30;365(6445):464-8. PMID:8413591
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