Cargando…
Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating
The proteasome is the central protease for intracellular protein breakdown. Coordinated binding and hydrolysis of ATP by the six proteasomal ATPase subunits induces conformational changes that drive the unfolding and translocation of substrates into the proteolytic 20S core particle for degradation....
Autores principales: | Eisele, Markus R., Reed, Randi G., Rudack, Till, Schweitzer, Andreas, Beck, Florian, Nagy, Istvan, Pfeifer, Gunter, Plitzko, Jürgen M., Baumeister, Wolfgang, Tomko, Robert J., Sakata, Eri |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6140342/ https://www.ncbi.nlm.nih.gov/pubmed/30067984 http://dx.doi.org/10.1016/j.celrep.2018.07.004 |
Ejemplares similares
-
Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle
por: Majumder, Parijat, et al.
Publicado: (2019) -
An Allosteric Interaction Network Promotes Conformation State-Dependent Eviction of the Nas6 Assembly Chaperone from Nascent 26S Proteasomes
por: Nemec, Antonia A., et al.
Publicado: (2019) -
Allosteric control of Ubp6 and the proteasome via a bidirectional switch
por: Hung, Ka Ying Sharon, et al.
Publicado: (2022) -
Wiggle and Shake: Managing and Exploiting Conformational Dynamics during Proteasome Biogenesis
por: Betancourt, Daniel, et al.
Publicado: (2023) -
Proteasomes tether to two distinct sites at the nuclear pore complex
por: Albert, Sahradha, et al.
Publicado: (2017)