Evidence map›Paper›PMID 26724270›Full record

ArticleJournal of structural biology2016

The LINKS motif zippers trans-acyltransferase polyketide synthase assembly lines into a biosynthetic megacomplex.

Darren C Gay, Drew T Wagner, Jessica L Meinke, Charles E Zogzas, Glen R Gay, Adrian T Keatinge-Clay

Abstract read
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In one paragraph

Article in Journal of structural biology, 2016. 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
–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

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Evolution-guided engineering ofScience (New York, N.Y.) · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Docking domain-mediated subunit interactions in natural product megasynth(et)ases.Journal of industrial microbiology & biotechnology · 2021
    Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. 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.

Darren C GayDepartment of Molecular Biosciences, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712-0165, United States.
Drew T WagnerDepartment of Molecular Biosciences, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712-0165, United States.
Jessica L MeinkeDepartment of Molecular Biosciences, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712-0165, United States.
Charles E ZogzasDepartment of Molecular Biosciences, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712-0165, United States.
Glen R GayDepartment of Molecular Biosciences, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712-0165, United States.
Adrian T Keatinge-ClayDepartment of Molecular Biosciences, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712-0165, United States; Department of Chemistry, The University of Texas at Austin, 1 University Station A5300, Austin, TX 78712-0165, United States. Electronic address: adriankc@utexas.edu.

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 GM106112NIGMS NIH HHS R01 GM106112
6 · The paper itself

Abstract

Polyketides such as the clinically-valuable antibacterial agent mupirocin are constructed by architecturally-sophisticated assembly lines known as trans-acyltransferase polyketide synthases. Organelle-sized megacomplexes composed of several copies of trans-acyltransferase polyketide synthase assembly lines have been observed by others through transmission electron microscopy to be located at the Bacillus subtilis plasma membrane, where the synthesis and export of the antibacterial polyketide bacillaene takes place. In this work we analyze ten crystal structures of trans-acyltransferase polyketide synthases ketosynthase domains, seven of which are reported here for the first time, to characterize a motif capable of zippering assembly lines into a megacomplex. While each of the three-helix LINKS (Laterally-INteracting Ketosynthase Sequence) motifs is observed to similarly dock with a spatially-reversed copy of itself through hydrophobic and ionic interactions, the amino acid sequences of this motif are not conserved. Such a code is appropriate for mediating homotypic contacts between assembly lines to ensure the ordered self-assembly of a noncovalent, yet tightly-knit, enzymatic network. LINKS-mediated lateral interactions would also have the effect of bolstering the vertical association of the polypeptides that comprise a polyketide synthase assembly line.

Indexed as

Amino Acid MotifsBacillus subtilisCrystallography, X-RayModels, MolecularMultiprotein ComplexesPolyenesPolyketide SynthasesProtein Structure, TertiarybacillaeneMultiprotein ComplexesPolyenesPolyketide SynthasesMegacomplexModular polyketide synthaseProtein–protein interactionX-ray crystallography

Identifiers

PMID26724270
PMCPMC4738151

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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.