Cargando…
A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin
The chaperonins (GroEL and GroES in Escherichia coli) are ubiquitous molecular chaperones that assist a subset of essential substrate proteins to undergo productive folding to the native state. Using single particle cryo EM and image processing we have examined complexes of E. coli GroEL with the st...
Autores principales: | Natesh, Ramanathan, Clare, Daniel K., Farr, George W., Horwich, Arthur L., Saibil, Helen R. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6096091/ https://www.ncbi.nlm.nih.gov/pubmed/29959019 http://dx.doi.org/10.1016/j.ijbiomac.2018.06.120 |
Ejemplares similares
-
Topologies of a Substrate Protein Bound to the Chaperonin GroEL
por: Elad, Nadav, et al.
Publicado: (2007) -
ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin
por: Clare, Daniel K., et al.
Publicado: (2012) -
Cryo-EM structures of GroEL:ES(2) with RuBisCO visualize molecular contacts of encapsulated substrates in a double-cage chaperonin
por: Kim, Hyunmin, et al.
Publicado: (2021) -
Folding of newly translated membrane protein CCR5 is assisted by the chaperonin
GroEL-GroES
por: Chi, Haixia, et al.
Publicado: (2015) -
Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction
por: Illingworth, Melissa, et al.
Publicado: (2017)