期刊
EMBO JOURNAL
卷 21, 期 18, 页码 4774-4784出版社
WILEY
DOI: 10.1093/emboj/cdf489
关键词
disulfide bond isomerase DsbC; electron transporter DsbD; oxidative protein folding; reaction intermediate; thiol oxidoreductase
资金
- NIGMS NIH HHS [GM55090, R01 GM055090] Funding Source: Medline
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 Angstrom 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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