Cargando…
ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP
AAA+ proteases perform regulated protein degradation in all kingdoms of life and consist of a hexameric AAA+ unfoldase/translocase in complex with a self-compartmentalized peptidase. Based on asymmetric features of cryo-EM structures and a sequential hand-over-hand model of substrate translocation,...
Autores principales: | Kim, Sora, Zuromski, Kristin L, Bell, Tristan A, Sauer, Robert T, Baker, Tania A |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7707817/ https://www.ncbi.nlm.nih.gov/pubmed/33258771 http://dx.doi.org/10.7554/eLife.61451 |
Ejemplares similares
-
Modular and coordinated activity of AAA+ active sites in the double-ring ClpA unfoldase of the ClpAP protease
por: Zuromski, Kristin L., et al.
Publicado: (2020) -
Division of labor between the pore-1 loops of the D1 and D2 AAA+ rings coordinates substrate selectivity of the ClpAP protease
por: Zuromski, Kristin L., et al.
Publicado: (2021) -
Antibiotic Acyldepsipeptides Stimulate the Streptomyces Clp-ATPase/ClpP Complex for Accelerated Proteolysis
por: Reinhardt, Laura, et al.
Publicado: (2022) -
Assembly and proteolytic processing of mycobacterial ClpP1 and ClpP2
por: Benaroudj, Nadia, et al.
Publicado: (2011) -
Lipopeptide biosynthesis in Pseudomonas fluorescens is regulated by the protease complex ClpAP
por: Song, Chunxu, et al.
Publicado: (2015)