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Highly dynamic interactions maintain kinetic stability of the ClpXP protease during the ATP-fueled mechanical cycle
The ClpXP protease assembles in a reaction in which an ATP-bound ring hexamer of ClpX binds to one or both heptameric rings of the ClpP peptidase. Contacts between ClpX IGF-loops and clefts on a ClpP ring stabilize the complex. How ClpXP stability is maintained during the ATP-hydrolysis cycle that p...
Shranjeno v:
| izdano v: | ACS Chem Biol |
|---|---|
| Main Authors: | , , , , |
| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
2016
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| Teme: | |
| Online dostop: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5087277/ https://ncbi.nlm.nih.gov/pubmed/27003103 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acschembio.6b00083 |
| Oznake: |
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