The structure of NAD
bacterial pathogenesis
hydrolase
innate immunity
nicotinamide adenine dinucleotide (NAD)
toll/interleukin-1 receptor (TIR)
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
Nov 2023
Nov 2023
Historique:
received:
25
05
2023
revised:
05
09
2023
accepted:
13
09
2023
medline:
27
11
2023
pubmed:
28
9
2023
entrez:
27
9
2023
Statut:
ppublish
Résumé
Toll-like and interleukin-1/18 receptor/resistance (TIR) domain-containing proteins function as important signaling and immune regulatory molecules. TIR domain-containing proteins identified in eukaryotic and prokaryotic species also exhibit NAD+ hydrolase activity in select bacteria, plants, and mammalian cells. We report the crystal structure of the Acinetobacter baumannii TIR domain protein (AbTir-TIR) with confirmed NAD
Identifiants
pubmed: 37758001
pii: S0021-9258(23)02318-9
doi: 10.1016/j.jbc.2023.105290
pmc: PMC10641520
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Deuterium
AR09D82C7G
Hydrolases
EC 3.-
NAD
0U46U6E8UK
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
105290Subventions
Organisme : NIGMS NIH HHS
ID : P30 GM133893
Pays : United States
Organisme : NIGMS NIH HHS
ID : R25 GM058264
Pays : United States
Organisme : NIGMS NIH HHS
ID : R25 GM119970
Pays : United States
Organisme : NIGMS NIH HHS
ID : T34 GM150447
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI172487
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM146694
Pays : United States
Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.