Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA
Protein disulfide bond formation in Escherichia coli is catalyzed by the periplasmic protein DsbA. A cytoplasmic membrane protein DsbB maintains DsbA in the oxidized state by transferring electrons from DsbA to quinones in the respiratory chain. Here we show that DsbB activity can be reconstituted b...
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| Vydáno v: | EMBO J |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Nature Publishing Group
2002
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC126001/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12006488/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/emboj/21.10.2354 |
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