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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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| Autors principals: | , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
2009
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| Matèries: | |
| Accés en línia: | 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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