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The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC–DsbDα complex
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 (DsbDα) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was t...
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| Main Authors: | , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Oxford University Press
2002
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC126285/ https://ncbi.nlm.nih.gov/pubmed/12234918 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/cdf489 |
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