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Crystal structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine

ClpX is a AAA+ machine that uses the energy of ATP binding and hydrolysis to unfold native proteins and translocate unfolded polypeptides into the ClpP peptidase. The crystal structures presented here reveal striking asymmetry in ring hexamers of nucleotide-free and nucleotide-bound ClpX. Asymmetry...

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Detaylı Bibliyografya
Asıl Yazarlar: Glynn, Steven E., Martin, Andreas, Nager, Andrew R., Baker, Tania A., Sauer, Robert T.
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 2009
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC2778613/
https://ncbi.nlm.nih.gov/pubmed/19914167
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.cell.2009.09.034
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