Evidence map›Paper›PMID 24362703›Full record

ArticleNature chemical biology2014

Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism.

Daniel P Dowling, Nathan A Bruender, Anthony P Young, Reid M McCarty, Vahe Bandarian, Catherine L Drennan

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
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

38 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  3. Article
  4. Article
  5. Review
  6. Cobalamin-Dependent RadicalACS bio & med chem Au · 2022
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Analysis of Electrochemical Properties ofJournal of the American Chemical Society · 2019
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

6 authors at 2 institutions in 1 country.

Daniel P Dowling1] Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA. [2] Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Nathan A BruenderDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona, USA.
Anthony P YoungDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona, USA.
Reid M McCartyDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona, USA.
Vahe BandarianDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona, USA.
Catherine L Drennan1] Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA. [2] Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA. [3] Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
University of Arizona · USMassachusetts Institute of Technology · US

Funding

X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN AP41RR012408 · NCRR · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI ORVILLE, ALLEN M · 1998 to 2011
$32.2M
Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Macromolecular Crystallography at the National Synchrotron Light SourceP41GM103473 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI SWEET, ROBERT M · 2012 to 2013
$4.9M
CHEMISTRY-BIOLOGY INTERFACE TRAINING PROGRAMT32GM008804 · NIGMS · UNIVERSITY OF ARIZONA · PI MONTFORT, WILLIAM R. · 2003 to 2023
$3.9M
Biosynthesis of Deazapurine-Containing MetabolitesR01GM072623 · NIGMS · UNIVERSITY OF UTAH · PI BANDARIAN, VAHE · 2005 to 2017
$3.9M
Howard Hughes Medical InstituteNCRR NIH HHS 5P41RR015301-10NCRR NIH HHS P41 RR012408NCRR NIH HHS P41RR012408NCRR NIH HHS P41 RR015301NIGMS NIH HHS 8 P41 GM103403-10NIGMS NIH HHS GM008804NIGMS NIH HHS GM72623NIGMS NIH HHS GM72623 S01NIGMS NIH HHS P41 GM103403NIGMS NIH HHS P41 GM103473NIGMS NIH HHS P41GM103473NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM072623NIGMS NIH HHS T32 GM008804
6 · The paper itself

Abstract

7-carboxy-7-deazaguanine synthase (QueE) catalyzes a key S-adenosyl-L-methionine (AdoMet)- and Mg(2+)-dependent radical-mediated ring contraction step, which is common to the biosynthetic pathways of all deazapurine-containing compounds. QueE is a member of the AdoMet radical superfamily, which employs the 5'-deoxyadenosyl radical from reductive cleavage of AdoMet to initiate chemistry. To provide a mechanistic rationale for this elaborate transformation, we present the crystal structure of a QueE along with structures of pre- and post-turnover states. We find that substrate binds perpendicular to the [4Fe-4S]-bound AdoMet, exposing its C6 hydrogen atom for abstraction and generating the binding site for Mg(2+), which coordinates directly to the substrate. The Burkholderia multivorans structure reported here varies from all other previously characterized members of the AdoMet radical superfamily in that it contains a hypermodified (β6/α3) protein core and an expanded cluster-binding motif, CX14CX2C.

Indexed as

Models, MolecularBinding SitesBurkholderiaFree RadicalsHydrogen BondingMagnesiumManganeseMolecular StructureProtein Structure, TertiaryS-AdenosylmethionineSodiumFree RadicalsMagnesiumManganeseS-AdenosylmethionineSodium

Identifiers

PMID24362703
PMCPMC3939041
OpenAlexW2080989975

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.