Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB

In the Escherichia coli system catalysing oxidative protein folding, disulphide bonds are generated by the cooperation of DsbB and ubiquinone and transferred to substrate proteins through DsbA. The structures solved so far for different forms of DsbB lack the Cys104–Cys130 initial-state disulphide t...

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Hlavní autoři: Inaba, Kenji, Murakami, Satoshi, Nakagawa, Atsushi, Iida, Hiroka, Kinjo, Mai, Ito, Koreaki, Suzuki, Mamoru
Médium: Artigo
Jazyk:Inglês
Vydáno: Nature Publishing Group 2009
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2666032/
https://ncbi.nlm.nih.gov/pubmed/19214188
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/emboj.2009.21
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