Evidence map›Paper›PMID 34735234›Full record

ArticleScience (New York, N.Y.)2021

Modular polyketide synthase contains two reaction chambers that operate asynchronously.

Saket R Bagde, Irimpan I Mathews, J Christopher Fromme, Chu-Young Kim

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

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  17. The structure of full-length AFPK supports the ACP linker in a role that regulates iterative polyketide and fatty acid assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

4 authors.

Saket R BagdeDepartment of Chemistry and Biochemistry, The University of Texas at El Paso, El Paso, TX 79968, USA.ORCID 0000-0001-9800-9326
Irimpan I MathewsStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, USA.ORCID 0000-0001-6254-3519
J Christopher FrommeDepartment of Molecular Biology and Genetics/Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0002-8837-0473
Chu-Young KimDepartment of Chemistry and Biochemistry, The University of Texas at El Paso, El Paso, TX 79968, USA.ORCID 0000-0003-3744-7802

Funding

UTEP Border Biomedical Research CenterU54MD007592 · NIMHD · UNIVERSITY OF TEXAS EL PASO · PI Gabriel Andrew Frietze · 2019 to 2026
$35.1M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
GTPase Regulation of the Golgi Complex (Diversity Supplement 2023)R35GM136258 · NIGMS · CORNELL UNIVERSITY · PI J Christopher Fromme · 2020 to 2026
$4.0M
Structural Biology of Polyether Antibiotic BiosynthesisR01GM138990 · NIGMS · UNIVERSITY OF TEXAS EL PASO · PI KIM, CHU-YOUNG · 2020 to 2024
$1.2M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM138990NIGMS NIH HHS R35 GM136258NIMHD NIH HHS U54 MD007592
6 · The paper itself

Abstract

Type I modular polyketide synthases are homodimeric multidomain assembly line enzymes that synthesize a variety of polyketide natural products by performing polyketide chain extension and β-keto group modification reactions. We determined the 2.4-angstrom-resolution x-ray crystal structure and the 3.1-angstrom-resolution cryo–electron microscopy structure of the Lsd14 polyketide synthase, stalled at the transacylation and condensation steps, respectively. These structures revealed how the constituent domains are positioned relative to each other, how they rearrange depending on the step in the reaction cycle, and the specific interactions formed between the domains. Like the evolutionarily related mammalian fatty acid synthase, Lsd14 contains two reaction chambers, but only one chamber in Lsd14 has the full complement of catalytic domains, indicating that only one chamber produces the polyketide product at any given time.

Indexed as

AcylationAcyl Carrier ProteinAcyltransferasesCatalytic DomainCryoelectron MicroscopyCrystallography, X-RayHydro-LyasesLasalocidModels, MolecularPolyketide SynthasesProtein ConformationProtein DomainsProtein MultimerizationStreptomycesAcyl Carrier ProteinAcyltransferasesHydro-LyasesLasalocidPolyketide Synthases

Identifiers

PMID34735234
PMCPMC8689591

What OpenQuestion holds

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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.