Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex.
Journal
Science (New York, N.Y.)
ISSN: 1095-9203
Titre abrégé: Science
Pays: United States
ID NLM: 0404511
Informations de publication
Date de publication:
24 04 2020
24 04 2020
Historique:
received:
22
12
2019
accepted:
16
03
2020
pubmed:
29
3
2020
medline:
15
5
2020
entrez:
29
3
2020
Statut:
ppublish
Résumé
Ribonucleotide reductases (RNRs) are a diverse family of enzymes that are alone capable of generating 2'-deoxynucleotides de novo and are thus critical in DNA biosynthesis and repair. The nucleotide reduction reaction in all RNRs requires the generation of a transient active site thiyl radical, and in class I RNRs, this process involves a long-range radical transfer between two subunits, α and β. Because of the transient subunit association, an atomic resolution structure of an active α2β2 RNR complex has been elusive. We used a doubly substituted β2, E52Q/(2,3,5)-trifluorotyrosine122-β2, to trap wild-type α2 in a long-lived α2β2 complex. We report the structure of this complex by means of cryo-electron microscopy to 3.6-angstrom resolution, allowing for structural visualization of a 32-angstrom-long radical transfer pathway that affords RNR activity.
Identifiants
pubmed: 32217749
pii: science.aba6794
doi: 10.1126/science.aba6794
pmc: PMC7774503
mid: NIHMS1657035
doi:
Substances chimiques
Escherichia coli Proteins
0
Holoenzymes
0
Tyrosine
42HK56048U
Ribonucleotide Reductases
EC 1.17.4.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
424-427Subventions
Organisme : NIGMS NIH HHS
ID : F32 GM123596
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM029595
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM126982
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States
Informations de copyright
Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.
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