Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients
The chaperone SurA is involved in outer membrane protein (OMP) biogenesis in Gram-negative bacteria, but its mechanism of action is not fully understood. Combining mass spectrometric, biophysical and computational approaches, the authors here show how the conformational dynamics of SurA facilitate O...
Guardado en:
Autores principales: | Antonio N. Calabrese, Bob Schiffrin, Matthew Watson, Theodoros K. Karamanos, Martin Walko, Julia R. Humes, Jim E. Horne, Paul White, Andrew J. Wilson, Antreas C. Kalli, Roman Tuma, Alison E. Ashcroft, David J. Brockwell, Sheena E. Radford |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2020
|
Materias: | |
Acceso en línea: | https://doaj.org/article/2047c9564bc341c98f0fa558c55a100a |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
por: Matthew G. Iadanza, et al.
Publicado: (2020) -
The Activity and Specificity of the Outer Membrane Protein Chaperone SurA Are Modulated by a Proline Isomerase Domain
por: Dante P. Ricci, et al.
Publicado: (2013) -
Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM
por: Matthew G. Iadanza, et al.
Publicado: (2016) -
Chaperone activation and client binding of a 2-cysteine peroxiredoxin
por: Filipa Teixeira, et al.
Publicado: (2019) -
Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state
por: Gefei Chen, et al.
Publicado: (2017)