Cargando…
Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX
The hexameric AAA+ ring of Escherichia. coli ClpX, an ATP-dependent protein unfolding and translocation machine, functions with the ClpP peptidase to degrade target substrates. For efficient function, ClpX subunits must switch between nucleotide-loadable (L) and nucleotide-unloadable (U) conformatio...
Autores principales: | Stinson, Benjamin M., Baytshtok, Vladimir, Schmitz, Karl R., Baker, Tania A., Sauer, Robert T. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4424054/ https://www.ncbi.nlm.nih.gov/pubmed/25866879 http://dx.doi.org/10.1038/nsmb.3012 |
Ejemplares similares
-
Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding
por: Martin, Andreas, et al.
Publicado: (2008) -
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) -
ClpX eats randomly
por: Wells, William A.
Publicado: (2005) -
The role of ClpX in erythropoietic protoporphyria
por: Whitman, Jared C., et al.
Publicado: (2018) -
Single molecule microscopy reveals diverse actions of substrate sequences that impair ClpX AAA+ ATPase function
por: Wang, Xiao, et al.
Publicado: (2022)