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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Bibliografiske detaljer

Udgivet i:	EMBO J
Principais autores:	Haebel, Peter W., Goldstone, David, Katzen, Federico, Beckwith, Jon, Metcalf, Peter
Format:	Artigo
Sprog:	Inglês
Udgivet:	Nature Publishing Group 2002
Fag:	Articles
Online adgang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC126285/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12234918/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/emboj/cdf489
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