Evidence map›Paper›PMID 27362945›Full record

ArticleACS chemical biology2016

Portability and Structure of the Four-Helix Bundle Docking Domains of trans-Acyltransferase Modular Polyketide Synthases.

Jia Zeng, Drew T Wagner, Zhicheng Zhang, Luisa Moretto, Janci D Addison, Adrian T Keatinge-Clay

Abstract read
In one paragraph

Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Direct Quantification of Protein-Protein Interactions in Living Bacterial Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  2. Article
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  4. Article
  5. Article
  6. Article
  7. Docking domain-mediated subunit interactions in natural product megasynth(et)ases.Journal of industrial microbiology & biotechnology · 2021
    Review
  8. Article
  9. 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.

Jia ZengDepartment of Molecular Biosciences and ‡Department of Chemistry, The University of Texas at Austin , Austin, Texas 78712, United States.
Drew T WagnerDepartment of Molecular Biosciences and ‡Department of Chemistry, The University of Texas at Austin , Austin, Texas 78712, United States.
Zhicheng ZhangDepartment of Molecular Biosciences and ‡Department of Chemistry, The University of Texas at Austin , Austin, Texas 78712, United States.
Luisa MorettoDepartment of Molecular Biosciences and ‡Department of Chemistry, The University of Texas at Austin , Austin, Texas 78712, United States.
Janci D AddisonDepartment of Molecular Biosciences and ‡Department of Chemistry, The University of Texas at Austin , Austin, Texas 78712, United States.
Adrian T Keatinge-ClayDepartment of Molecular Biosciences and ‡Department of Chemistry, The University of Texas at Austin , Austin, Texas 78712, United States.

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
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM106112
6 · The paper itself

Abstract

The polypeptides of multimodular polyketide synthases self-assemble into biosynthetic factories. While the docking domains that mediate the assembly of cis-acyltransferase polyketide synthase polypeptides are well-studied, those of the more recently discovered trans-acyltransferase polyketide synthases have just started to be described. Located at the C- and N-termini of many polypeptides, these 25-residue, two-helix, pseudosymmetric motifs noncovalently connect domains both between and within modules. Domains expressed with their natural, cognate docking motifs formed complexes stable to size-exclusion chromatography with 1-10 μM dissociation constants as measured by isothermal titration calorimetry. Deletion and swapping experiments demonstrate portability of the docking motifs. A 1.72 Å-resolution structure of the N-terminal portion of the macrolactin synthase polypeptide MlnE shows an uncomplexed N-terminal docking motif to be preorganized in the conformation it assumes within the docking domain complex.

Indexed as

AcyltransferasesCrystallography, X-RayModels, MolecularPolyketide SynthasesAcyltransferasesPolyketide Synthases

Identifiers

PMID27362945
PMCPMC5460766

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.