Evidence map›Paper›PMID 38968292›Full record

ArticleeLife2024

Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding.

Ornella Bimai, Ipsita Banerjee, Inna Rozman Grinberg, Ping Huang, Lucas Hultgren, Simon Ekström, Daniel Lundin, Britt-Marie Sjöberg, Derek T Logan

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Ornella BimaiDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID https://orcid.org/0000-0003-0562-7251
Ipsita BanerjeeSection for Biochemistry and Structural Biology, Centre for Molecular Protein Science, Department of Chemistry, Lund University, Lund, Sweden.
Inna Rozman GrinbergDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID https://orcid.org/0000-0003-3094-1998
Ping HuangDepartment of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.ORCID https://orcid.org/0000-0002-7676-6905
Lucas HultgrenStructural Proteomics, SciLifeLab, Lund University, Lund, Sweden.
Simon EkströmStructural Proteomics, SciLifeLab, Lund University, Lund, Sweden.ORCID https://orcid.org/0000-0002-7694-285X
Daniel LundinDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID https://orcid.org/0000-0002-8779-6464
Britt-Marie SjöbergDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID https://orcid.org/0000-0001-5953-3360
Derek T LoganSection for Biochemistry and Structural Biology, Centre for Molecular Protein Science, Department of Chemistry, Lund University, Lund, Sweden.ORCID https://orcid.org/0000-0002-0098-8560

Funding

Cancerfonden CAN 20 1210 PjFVetenskapsrådet 2016-04855Vetenskapsrådet 2019-01400
6 · The paper itself

Abstract

A small, nucleotide-binding domain, the ATP-cone, is found at the N-terminus of most ribonucleotide reductase (RNR) catalytic subunits. By binding adenosine triphosphate (ATP) or deoxyadenosine triphosphate (dATP) it regulates the enzyme activity of all classes of RNR. Functional and structural work on aerobic RNRs has revealed a plethora of ways in which dATP inhibits activity by inducing oligomerisation and preventing a productive radical transfer from one subunit to the active site in the other. Anaerobic RNRs, on the other hand, store a stable glycyl radical next to the active site and the basis for their dATP-dependent inhibition is completely unknown. We present biochemical, biophysical, and structural information on the effects of ATP and dATP binding to the anaerobic RNR from

Indexed as

Adenosine TriphosphateProtein BindingRibonucleotide ReductasesAllosteric RegulationAnaerobiosisCatalytic DomainDeoxyadenine NucleotidesModels, MolecularProtein ConformationProtein MultimerizationSubstrate Specificity2'-deoxyadenosine triphosphateAdenosine TriphosphateDeoxyadenine NucleotidesRibonucleotide Reductasesallosteric regulationATP-conebiochemistrychemical biologyglycyl radicalPrevotella copriribonucleotide reductase

Identifiers

PMID38968292
PMCPMC11226230

What OpenQuestion holds

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Registered trials

None linked

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.