Crystal structure of the periplasmic sensor domain of histidine kinase VbrK suggests indirect sensing of β-lactam antibiotics.
Histidine kinase
Sensing domain
Single wavelength anomalous dispersion
Two component system
Vibrio
Journal
Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206
Informations de publication
Date de publication:
01 11 2020
01 11 2020
Historique:
received:
12
07
2020
revised:
19
08
2020
accepted:
26
08
2020
pubmed:
6
9
2020
medline:
15
10
2021
entrez:
5
9
2020
Statut:
ppublish
Résumé
Bacterial two-component regulatory systems (TCS) play important roles in sensing environmental stimuli and responding to them by regulating gene expression. VbrK/VbrR, a TCS in Vibrio parahaemolyticus, confers resistance to β-lactam antibiotics through activating a β-lactamase gene. Its periplasmic sensor domain was previously suggested to detect β-lactam antibiotics by direct binding. Here, we report a crystal structure of the periplasmic sensing domain of VbrK (VbrK
Identifiants
pubmed: 32890780
pii: S1047-8477(20)30183-0
doi: 10.1016/j.jsb.2020.107610
pii:
doi:
Substances chimiques
Anti-Bacterial Agents
0
Bacterial Proteins
0
beta-Lactams
0
Histidine Kinase
EC 2.7.13.1
beta-Lactamases
EC 3.5.2.6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
107610Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.