1jzd
From Proteopedia
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[[Image:1jzd.gif|left|200px]] | [[Image:1jzd.gif|left|200px]] | ||
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'''DsbC-DsbDalpha complex''' | '''DsbC-DsbDalpha complex''' | ||
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[[Category: Katzen, F.]] | [[Category: Katzen, F.]] | ||
[[Category: Metcalf, P.]] | [[Category: Metcalf, P.]] | ||
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| - | [[Category: | + | [[Category: Thiol disulfide oxidoreductase]] |
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Revision as of 19:06, 2 May 2008
DsbC-DsbDalpha complex
Overview
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.
About this Structure
1JZD is a Protein complex structure of sequences 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 Page seeded by OCA on Fri May 2 22:06:31 2008
