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Title3.3-Å resolution cryo-EM structure of human ribonucleotide reductase with substrate and allosteric regulators bound.
Journal, issue, pagesElife, Vol. 7, Year 2018
Publish dateFeb 20, 2018
AuthorsEdward J Brignole / Kuang-Lei Tsai / Johnathan Chittuluru / Haoran Li / Yimon Aye / Pawel A Penczek / JoAnne Stubbe / Catherine L Drennan / Francisco Asturias /
PubMed AbstractRibonucleotide reductases (RNRs) convert ribonucleotides into deoxyribonucleotides, a reaction essential for DNA replication and repair. Human RNR requires two subunits for activity, the α subunit ...Ribonucleotide reductases (RNRs) convert ribonucleotides into deoxyribonucleotides, a reaction essential for DNA replication and repair. Human RNR requires two subunits for activity, the α subunit contains the active site, and the β subunit houses the radical cofactor. Here, we present a 3.3-Å resolution structure by cryo-electron microscopy (EM) of a dATP-inhibited state of human RNR. This structure, which was determined in the presence of substrate CDP and allosteric regulators ATP and dATP, has three α units arranged in an α ring. At near-atomic resolution, these data provide insight into the molecular basis for CDP recognition by allosteric specificity effectors dATP/ATP. Additionally, we present lower-resolution EM structures of human α in the presence of both the anticancer drug clofarabine triphosphate and β. Together, these structures support a model for RNR inhibition in which β is excluded from binding in a radical transfer competent position when α exists as a stable hexamer.
External linksElife / PubMed:29460780 / PubMed Central
MethodsEM (single particle)
Resolution3.3 Å
Structure data

7006

6aui

EMDB-7006, PDB-6aui:
Human ribonucleotide reductase large subunit (alpha) with dATP and CDP
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-DTP:
2'-DEOXYADENOSINE 5'-TRIPHOSPHATE / Deoxyadenosine triphosphate

ChemComp-MG:
Unknown entry

ChemComp-CDP:
CYTIDINE-5'-DIPHOSPHATE / Cytidine diphosphate

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / Ribonucleotide Reductase Electron transfer Radical chemistry Thiyl radical

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