Evidence map›Paper›PMID 25129028›Full record

ArticleNature chemical biology2014

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

Kyle L Dunbar, Jonathan R Chekan, Courtney L Cox, Brandon J Burkhart, Satish K Nair, Douglas A Mitchell

Abstract 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 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. Article
  2. Article
  3. ThiF-Like Enzyme Chemistry in Primary and Secondary Metabolism.Chembiochem : a European journal of chemical biology · 2025
    Review
  4. Article
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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.

Kyle L Dunbar1] Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA. [2] Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA. [3].
Jonathan R Chekan1] Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA. [2].
Courtney L Cox1] Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA. [2] Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Brandon J Burkhart1] Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA. [2] Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Satish K Nair1] Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA. [2] Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA. [3] Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Douglas A Mitchell1] Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA. [2] Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA. [3] Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.

Funding

Training Program in Chemistry-Interface with BiologyT32GM070421 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HERGENROTHER, PAUL · 2005 to 2019
$5.4M
Enzyme Chemistry and Biological Function of RiPP-like Modifications.R01GM097142 · NIGMS · VANDERBILT UNIVERSITY · PI MITCHELL, DOUGLAS ALAN · 2012 to 2024
$4.1M
Directed posttranslational modifications for drug design and discoveryR01GM102602 · NIGMS · UNIVERSITY OF UTAH · PI SCHMIDT, ERIC W · 2013 to 2016
$1.4M
4800 Plus MALDI TOF/TOF AnalyzerS10RR027109 · NCRR · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 2010 to 2010
$395k
NCRR NIH HHS S10 RR027109NCRR NIH HHS S10 RR027109 ANIGMS NIH HHS 1R01 GM097142NIGMS NIH HHS 1R01 GM102602NIGMS NIH HHS 2T32 GM070421NIGMS NIH HHS R01 GM097142NIGMS NIH HHS R01 GM102602NIGMS NIH HHS T32 GM070421
6 · The paper itself

Abstract

Despite intensive research, the cyclodehydratase responsible for azoline biogenesis in thiazole/oxazole-modified microcin (TOMM) natural products remains enigmatic. The collaboration of two proteins, C and D, is required for cyclodehydration. The C protein is homologous to E1 ubiquitin-activating enzymes, whereas the D protein is within the YcaO superfamily. Recent studies have demonstrated that TOMM YcaOs phosphorylate amide carbonyl oxygens to facilitate azoline formation. Here we report the X-ray crystal structure of an uncharacterized YcaO from Escherichia coli (Ec-YcaO). Ec-YcaO harbors an unprecedented fold and ATP-binding motif. This motif is conserved among TOMM YcaOs and is required for cyclodehydration. Furthermore, we demonstrate that the C protein regulates substrate binding and catalysis and that the proline-rich C terminus of the D protein is involved in C protein recognition and catalysis. This study identifies the YcaO active site and paves the way for the characterization of the numerous YcaO domains not associated with TOMM biosynthesis.

Indexed as

Adenosine TriphosphateAmino Acid MotifsBacteriocinsCatalytic DomainCrystallography, X-RayEscherichia coliEscherichia coli ProteinsHydro-LyasesModels, MolecularMolecular Sequence DataOxazolesPhosphotransferasesProtein BindingProtein BiosynthesisProtein FoldingProtein Structure, SecondaryAdenosine TriphosphateBacteriocinsEscherichia coli ProteinsHydro-LyasesmicrocinOxazolesPhosphotransferasesThiazolesUbiquitin-Activating Enzymes

Identifiers

PMID25129028
PMCPMC4167974

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.