1dsb: Difference between revisions
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'''CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR DISULPHIDE BOND FORMATION IN VIVO''' | {{Structure | ||
|PDB= 1dsb |SIZE=350|CAPTION= <scene name='initialview01'>1dsb</scene>, resolution 2.0Å | |||
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'''CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR DISULPHIDE BOND FORMATION IN VIVO''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DSB is a [ | 1DSB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSB OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8413591 8413591] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: disulfide oxidoreductase]] | [[Category: disulfide oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:43:30 2008'' | ||
Revision as of 11:43, 20 March 2008
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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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