Evidence map›Paper›PMID 28625788›Full record

ArticleStructure (London, England : 1993)2017

Structural and Functional Trends in Dehydrating Bimodules from trans-Acyltransferase Polyketide Synthases.

Drew T Wagner, Jia Zeng, Constance B Bailey, Darren C Gay, Fang Yuan, Hannah R Manion, Adrian T Keatinge-Clay

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 27 citations in OpenAlex.

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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

7 authors at 1 institution in 1 country.

Drew T WagnerDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA.
Jia ZengDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA.
Constance B BaileyDepartment of Chemistry, University of Texas at Austin, Austin, TX 78712, USA.
Darren C GayDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA.
Fang YuanDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA.
Hannah R ManionDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA.
Adrian T Keatinge-ClayDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA; Department of Chemistry, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: adriankc@utexas.edu.
The University of Texas at Austin · US

Funding

Determining the Architectures and Activities of Polyketide Synthase ModulesR01GM106112 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI KEATINGE-CLAY, ADRIAN TRISTAN · 2013 to 2025
$3.9M
NIGMS NIH HHS R01 GM106112
6 · The paper itself

Abstract

In an effort to uncover the structural motifs and biosynthetic logic of the relatively uncharacterized trans-acyltransferase polyketide synthases, we have begun the dissection of the enigmatic dehydrating bimodules common in these enzymatic assembly lines. We report the 1.98 Å resolution structure of a ketoreductase (KR) from the first half of a type A dehydrating bimodule and the 2.22 Å resolution structure of a dehydratase (DH) from the second half of a type B dehydrating bimodule. The KR, from the third module of the bacillaene synthase, and the DH, from the tenth module of the difficidin synthase, possess features not observed in structurally characterized homologs. The DH architecture provides clues for how it catalyzes a unique double dehydration. Correlations between the chemistries proposed for dehydrating bimodules and bioinformatic analysis indicate that type A dehydrating bimodules generally produce an α/β-cis alkene moiety, while type B dehydrating bimodules generally produce an α/β-trans, γ/δ-cis diene moiety.

Indexed as

AcyltransferasesAlcohol OxidoreductasesBacillusBacterial ProteinsPolyketide SynthasesAcyltransferasesAlcohol OxidoreductasesBacterial Proteinspolyketide synthase ketoreductasePolyketide Synthasesassembly line architecturebioinformaticsdehydratasedehydrating bimoduledouble dehydrationketoreductasemodular polyketide synthasepolyketidetrans-acyltransferase polyketide synthaseX-ray crystallography

Identifiers

PMID28625788
PMCPMC5553570
OpenAlexW2626241739

What OpenQuestion holds

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LicenceTDM
Read underepoch 390

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.