Evidence map›Paper›PMID 21707057›Full record

ArticleBiochemistry2011

Structure and mechanism of the trans-acting acyltransferase from the disorazole synthase.

Fong T Wong, Xi Jin, Irimpan I Mathews, David E Cane, Chaitan Khosla

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

42 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Prokaryotic PfaB is a terminal acyltransferase that determines the final PUFA product.Protein science : a publication of the Protein Society · 2026
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  9. Interfacial plasticity facilitates high reaction rate ofProceedings of the National Academy of Sciences of the United States of America · 2020
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  15. Review
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  19. Elucidating the mechanism of fluorinated extender unit loading for improved production of fluorine-containing polyketides.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. 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

5 authors at 2 institutions in 1 country.

Fong T WongDepartment of Chemical Engineering, Department of Chemistry, and §Department of Biochemistry, Stanford University , Stanford, California 94305, United States.
Xi Jin
Irimpan I Mathews
David E Cane
Chaitan Khosla
Brown University · USStanford University · US

Funding

BIOSYNTHESIS OF MICROBIAL PRODUCTSR01GM022172 · NIGMS · BROWN UNIVERSITY · PI CANE, DAVID E · 1985 to 2017
$5.7M
Structure, Mechanism, and Engineering of Assembly Line Polyketide SynthasesR01GM087934 · NIGMS · STANFORD UNIVERSITY · PI KHOSLA, CHAITAN · 2009 to 2021
$4.9M
NIGMS NIH HHS GM022172NIGMS NIH HHS GM087934NIGMS NIH HHS R01 GM022172NIGMS NIH HHS R01 GM087934
6 · The paper itself

Abstract

The 1.51 Å resolution X-ray crystal structure of the trans-acyltransferase (AT) from the "AT-less" disorazole synthase (DSZS) and that of its acetate complex at 1.35 Å resolution are reported. Separately, comprehensive alanine-scanning mutagenesis of one of its acyl carrier protein substrates (ACP1 from DSZS) led to the identification of a conserved Asp45 residue on the ACP, which contributes to the substrate specificity of this unusual enzyme. Together, these experimental findings were used to derive a model for the selective association of the DSZS AT and its ACP substrate. With a goal of structurally characterizing the AT-ACP interface, a strategy was developed for covalently cross-linking the active site Ser → Cys mutant of the DSZS AT to its ACP substrate and for purifying the resulting AT-ACP complex to homogeneity. The S86C DSZS AT mutant was found to be functional, albeit with a transacylation efficiency 200-fold lower than that of its wild-type counterpart. Our findings provide new insights as well as new opportunities for high-resolution analysis of an important protein-protein interface in polyketide synthases.

Indexed as

Acyl Carrier ProteinAcyltransferasesAlanineAmino Acid SequenceCrystallizationCrystallography, X-RayEscherichia coli ProteinsFatty Acid SynthasesMacrolidesMolecular Sequence DataMutagenesis, Site-DirectedOxazolesProtein Structure, TertiaryStreptomyces coelicolorStructure-Activity RelationshipSubstrate SpecificityAcyl Carrier ProteinAcyltransferasesAlanineEscherichia coli ProteinsFatty Acid SynthasesMacrolidesOxazoles

Identifiers

PMID21707057
PMCPMC3144309
OpenAlexW2110553113

What OpenQuestion holds

Textmetadata
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.