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The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1
Clp chaperone-proteases are cylindrical complexes built from ATP-dependent chaperone rings that stack onto a proteolytic ClpP double-ring core to carry out substrate protein degradation. Interaction of the ClpP particle with the chaperone is mediated by an N-terminal loop and a hydrophobic surface p...
Tallennettuna:
| Julkaisussa: | PLoS One |
|---|---|
| Päätekijät: | , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Public Library of Science
2015
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4416901/ https://ncbi.nlm.nih.gov/pubmed/25933022 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0125345 |
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