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Both ATPase Domains of ClpA Are Critical for Processing of Stable Protein Structures
ClpA is a ring-shaped hexameric chaperone that binds to both ends of the protease ClpP and catalyzes the ATP-dependent unfolding and translocation of substrate proteins through its central pore into the ClpP cylinder. Here we study the relevance of ATP hydrolysis in the two ATPase domains of ClpA. W...
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| Autors principals: | , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
American Society for Biochemistry and Molecular Biology
2009
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2781540/ https://ncbi.nlm.nih.gov/pubmed/19726681 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.022319 |
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