The structure of DarB in complex with Rel
Journal
Science advances
ISSN: 2375-2548
Titre abrégé: Sci Adv
Pays: United States
ID NLM: 101653440
Informations de publication
Date de publication:
18 Jan 2023
18 Jan 2023
Historique:
entrez:
18
1
2023
pubmed:
19
1
2023
medline:
19
1
2023
Statut:
ppublish
Résumé
Rel stringent factors are bifunctional ribosome-associated enzymes that catalyze both synthesis and hydrolysis of the alarmones (p)ppGpp. Besides the allosteric control by starved ribosomes and (p)ppGpp, Rel is regulated by various protein factors depending on specific stress conditions, including the c-di-AMP-binding protein DarB. However, how these effector proteins control Rel remains unknown. We have determined the crystal structure of the DarB
Identifiants
pubmed: 36652515
doi: 10.1126/sciadv.ade4077
pmc: PMC9848473
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
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