Coupling of zinc and GTP binding drives G-domain folding in Acinetobacter baumannii ZigA.
Journal
Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626
Informations de publication
Date de publication:
08 Mar 2024
08 Mar 2024
Historique:
received:
09
01
2024
revised:
22
02
2024
accepted:
05
03
2024
pubmed:
9
3
2024
medline:
9
3
2024
entrez:
9
3
2024
Statut:
aheadofprint
Résumé
COG0523 proteins, also known as nucleotide-dependent metallochaperones, are a poorly understood class of small P-loop G3E GTPases. Multiple family members play critical roles in bacterial pathogen survival during an infection as part of the adaptive response to host-mediated "nutritional immunity." Our understanding of the structure, dynamics, and molecular-level function of COG0523 proteins, apart from the eukaryotic homolog, Zng1, remains in its infancy. Here, we use X-ray absorption spectroscopy to establish that Acinetobacter baumannii (Ab) ZigA coordinates Zn
Identifiants
pubmed: 38459695
pii: S0006-3495(24)00175-9
doi: 10.1016/j.bpj.2024.03.010
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIAID NIH HHS
ID : R01 AI101171
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM118157
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM131994
Pays : United States
Informations de copyright
Copyright © 2024 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.