Solution Structure of the dATP-Inactivated Class I Ribonucleotide Reductase From
allosteric regulation
nucleotide binding
oligomerization
ribonucleotide reductase
single particle cryo-EM
small-angle X-ray scattering
Journal
Frontiers in molecular biosciences
ISSN: 2296-889X
Titre abrégé: Front Mol Biosci
Pays: Switzerland
ID NLM: 101653173
Informations de publication
Date de publication:
2021
2021
Historique:
received:
23
05
2021
accepted:
21
06
2021
entrez:
12
8
2021
pubmed:
13
8
2021
medline:
13
8
2021
Statut:
epublish
Résumé
The essential enzyme ribonucleotide reductase (RNR) is highly regulated both at the level of overall activity and substrate specificity. Studies of class I, aerobic RNRs have shown that overall activity is downregulated by the binding of dATP to a small domain known as the ATP-cone often found at the N-terminus of RNR subunits, causing oligomerization that prevents formation of a necessary α
Identifiants
pubmed: 34381817
doi: 10.3389/fmolb.2021.713608
pii: 713608
pmc: PMC8350387
doi:
Types de publication
Journal Article
Langues
eng
Pagination
713608Informations de copyright
Copyright © 2021 Hasan, Banerjee, Rozman Grinberg, Sjöberg and Logan.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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