Cargando…
Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor
ATPases of the AAA+ superfamily are large oligomeric molecular machines that remodel their substrates by converting the energy from ATP hydrolysis into mechanical force. This study focuses on the molecular chaperone ClpB, the bacterial homologue of Hsp104, which reactivates aggregated proteins under...
Autores principales: | Zeymer, Cathleen, Barends, Thomas R. M., Werbeck, Nicolas D., Schlichting, Ilme, Reinstein, Jochen |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3940203/ https://www.ncbi.nlm.nih.gov/pubmed/24531492 http://dx.doi.org/10.1107/S1399004713030629 |
Ejemplares similares
-
trans-Acting Arginine Residues in the AAA+ Chaperone ClpB Allosterically Regulate the Activity through Inter- and Intradomain Communication
por: Zeymer, Cathleen, et al.
Publicado: (2014) -
Dynamic structural states of ClpB involved in its disaggregation function
por: Uchihashi, Takayuki, et al.
Publicado: (2018) -
Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase
por: Rizo, Alexandrea N., et al.
Publicado: (2019) -
Publisher Correction: Dynamic structural states of ClpB involved in its disaggregation function
por: Uchihashi, Takayuki, et al.
Publicado: (2019) -
Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions
por: Duran, Elizabeth C., et al.
Publicado: (2017)