1jzo

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[[Image:1jzo.gif|left|200px]]
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{{STRUCTURE_1jzo| PDB=1jzo | SCENE= }}
{{STRUCTURE_1jzo| PDB=1jzo | SCENE= }}
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'''DsbC C101S'''
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===DsbC C101S===
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==Overview==
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The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDalpha) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was trapped, yielding a covalent DsbC-DsbDalpha complex. The 2.3 A crystal structure of the complex shows for the first time the specific interactions between two thiol oxidoreductases. DsbDalpha is a novel thiol oxidoreductase with the active site cysteines embedded in an immunoglobulin fold. It binds into the central cleft of the V-shaped DsbC dimer, which assumes a closed conformation on complex formation. Comparison of the complex with oxidized DsbDalpha reveals major conformational changes in a cap structure that regulates the accessibility of the DsbDalpha active site. Our results explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm.
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(as it appears on PubMed at http://www.pubmed.gov), where 12234918 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12234918}}
==About this Structure==
==About this Structure==
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[[Category: Thiol oxidoreductase]]
[[Category: Thiol oxidoreductase]]
[[Category: Thioredoxin fold]]
[[Category: Thioredoxin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:50:39 2008''

Revision as of 16:50, 28 July 2008

Template:STRUCTURE 1jzo

DsbC C101S

Template:ABSTRACT PUBMED 12234918

About this Structure

1JZO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex., Haebel PW, Goldstone D, Katzen F, Beckwith J, Metcalf P, EMBO J. 2002 Sep 16;21(18):4774-84. PMID:12234918

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