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| [[Image:1jzd.gif|left|200px]] | | {{Seed}} |
| | [[Image:1jzd.png|left|200px]] |
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| {{STRUCTURE_1jzd| PDB=1jzd | SCENE= }} | | {{STRUCTURE_1jzd| PDB=1jzd | SCENE= }} |
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| '''DsbC-DsbDalpha complex'''
| | ===DsbC-DsbDalpha complex=== |
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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. | | The line below this paragraph, {{ABSTRACT_PUBMED_12234918}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12234918 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12234918}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Reaction intermediate]] | | [[Category: Reaction intermediate]] |
| [[Category: Thiol disulfide oxidoreductase]] | | [[Category: Thiol disulfide oxidoreductase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:06:31 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:29:57 2008'' |