Structural Dynamics of the Functional Nonameric Type III Translocase Export Gate.
Adenosine Triphosphatases
/ chemistry
Allosteric Regulation
Binding Sites
Cloning, Molecular
Cryoelectron Microscopy
Deuterium Exchange Measurement
Enteropathogenic Escherichia coli
/ genetics
Escherichia coli Proteins
/ chemistry
Flagella
/ genetics
Gene Expression
Gene Expression Regulation, Bacterial
Genetic Vectors
/ chemistry
Kinetics
Mass Spectrometry
Models, Molecular
Molecular Chaperones
/ chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Subunits
/ chemistry
Recombinant Proteins
/ chemistry
SEC Translocation Channels
/ chemistry
Substrate Specificity
Type III Secretion Systems
/ genetics
EPEC
SctV-C structure
export apparatus
protein dynamics
type III secretion
Journal
Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R
Informations de publication
Date de publication:
15 10 2021
15 10 2021
Historique:
received:
10
06
2021
revised:
30
07
2021
accepted:
02
08
2021
pubmed:
30
8
2021
medline:
25
11
2021
entrez:
29
8
2021
Statut:
ppublish
Résumé
Type III protein secretion is widespread in Gram-negative pathogens. It comprises the injectisome with a surface-exposed needle and an inner membrane translocase. The translocase contains the SctRSTU export channel enveloped by the export gate subunit SctV that binds chaperone/exported clients and forms a putative ante-chamber. We probed the assembly, function, structure and dynamics of SctV from enteropathogenic E. coli (EPEC). In both EPEC and E. coli lab strains, SctV forms peripheral oligomeric clusters that are detergent-extracted as homo-nonamers. Membrane-embedded SctV
Identifiants
pubmed: 34454944
pii: S0022-2836(21)00421-6
doi: 10.1016/j.jmb.2021.167188
pii:
doi:
Substances chimiques
Escherichia coli Proteins
0
Molecular Chaperones
0
Protein Subunits
0
Recombinant Proteins
0
SEC Translocation Channels
0
Type III Secretion Systems
0
Adenosine Triphosphatases
EC 3.6.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
167188Informations de copyright
Crown Copyright © 2021. Published by Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Competing interests The authors declare they have no competing financial interests or other conflicts of interest