Evidence map›Paper›PMID 39416103›Full record

ArticlebioRxiv : the preprint server for biology2024

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 readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Dana E WestmorelandDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.ORCID 0000-0002-5728-2446
Patricia R FelicianoHoward Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139.
Gyunghoon KangHoward Hughes Medical Institute, 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.
Daniel G NoceraDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138.
Catherine L DrennanHoward Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139.

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
NIGMS 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

cryogenic electron microscopyenzyme inhibitionproton-coupled electron transferRadical chemistry

Identifiers

PMID39416103
PMCPMC11482829

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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.