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Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding

Proteolytic AAA+ unfoldases use ATP hydrolysis to power conformational changes that mechanically denature protein substrates and then translocate the polypeptide through a narrow pore into a degradation chamber. We show that a tyrosine in a pore loop of the hexameric ClpX unfoldase links ATP hydroly...

詳細記述

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書誌詳細
主要な著者: Martin, Andreas, Baker, Tania A., Sauer, Robert T.
フォーマット: Artigo
言語:Inglês
出版事項: 2008
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC2610342/
https://ncbi.nlm.nih.gov/pubmed/18931677
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/nsmb.1503
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