Evidence map›Paper›PMID 39475643›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2024

2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor N

Dana E Westmoreland, Patricia R Feliciano, Gyunghoon Kang, Chang Cui, Albert Kim, JoAnne Stubbe, Daniel G Nocera, Catherine L Drennan

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Low-barrier hydrogen bond powers long-range radical transfer in the metal-free ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Allosteric gating of radical transport in ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. 50 Years of Giese Reaction - a Personal View.Angewandte Chemie (International ed. in English) · 2026
    Review
  9. Conformationally gated multisite proton-coupled electron transfer in the ribonucleotide reductaseProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. Article
  12. Profile of Catherine Drennan.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Dana E Westmoreland *Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.
Patricia R Feliciano *Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.ORCID 0000-0003-3853-115X
Gyunghoon KangDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.
Chang CuiDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.
Albert KimDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.
JoAnne StubbeDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.ORCID 0000-0001-8076-4489
Daniel G NoceraDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138.ORCID 0000-0001-5055-320X
Catherine L DrennanDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.ORCID 0000-0001-5486-2755

Funding

Structure-Function Studies of Ribonucleotide ReductaseR01GM047274 · NIGMS · MICHIGAN STATE UNIVERSITY · PI DANIEL G. NOCERA · 1992 to 2026
$9.9M
Ribonucleotide Reductase: Structure and FunctionR01GM029595 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI STUBBE, JOANNE · 1985 to 2016
$6.9M
Metalloenzyme structure, function and assemblyR35GM126982 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI CATHERINE L DRENNAN · 2018 to 2026
$3.4M
Structure function investigations of radical transfer and disulfide exchange in a class Ia ribonucleotide reductaseF32GM145072 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WESTMORELAND, DANA · 2022 to 2024
$213k
MECHANISM OF DINUCLEAR FE-Y. FORMATION OF NDP REDUCTASER37GM029595 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI STUBBE, JOANNE · 1988 to 1997
–
HHS | NIH | National Institute of General Medical Sciences (NIGMS) GM047274HHS | NIH | National Institute of General Medical Sciences (NIGMS) GM126982HHS | NIH | National Institute of General Medical Sciences (NIGMS) GM29595Howard Hughes Medical Institute (HHMI) InvestigatorNIGMS NIH HHS F32 GM145072NIGMS NIH HHS R01 GM029595NIGMS NIH HHS R01 GM047274NIGMS NIH HHS R35 GM126982
6 · The paper itself

Abstract

Ribonucleotide reductases (RNRs) reduce ribonucleotides to deoxyribonucleotides using radical-based chemistry. For class Ia RNRs, the radical species is stored in a separate subunit (β2) from the subunit housing the active site (α2), requiring the formation of a short-lived α2β2 complex and long-range radical transfer (RT). RT occurs via proton-coupled electron transfer (PCET) over a long distance (~32-Å) and involves the formation and decay of multiple amino acid radical species. Here, we use cryogenic electron microscopy and a mechanism-based inhibitor 2'-azido-2'-deoxycytidine-5'-diphosphate (N

Indexed as

Cryoelectron MicroscopyEscherichia coliRibonucleotide ReductasesCatalytic DomainCytidine DiphosphateEnzyme InhibitorsEscherichia coli ProteinsModels, MolecularCytidine DiphosphateEnzyme InhibitorsEscherichia coli ProteinsRibonucleotide Reductasescryogenic electron microscopyenzyme inhibitionproton-coupled electron transferradical chemistry

Identifiers

PMID39475643
PMCPMC11551348

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.