Evidence map›Paper›PMID 25791608›Full record

ReviewCurrent opinion in structural biology2015

Architecture of the polyketide synthase module: surprises from electron cryo-microscopy.

Janet L Smith, Georgios Skiniotis, David H Sherman

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.2field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. More than a colour; how pigment influences colourblind microbes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Recent trends in biocatalysis.Chemical Society reviews · 2021
    Review
  9. Review
  10. Article
  11. Review
  12. Cryo-EM: beyond the microscope.Current opinion in structural biology · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Polyproteins in structural biology.Current opinion in structural biology · 2015
    Review
  20. Review
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

3 authors at 1 institution in 1 country.

Janet L SmithLife Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: JanetSmith@umich.edu.
Georgios SkiniotisLife Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
David H ShermanLife Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA; Department of Medicinal Chemistry, University of Michigan, Ann Arbor, MI 48109, USA; Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA; Department of Microbiology & Immunology, University of Michigan, Ann Arbor, MI 48109, USA.
University of Michigan–Ann Arbor · US

Funding

STRUCTURE AND FUNCTION OF A PURINE BIOSYNTHETIC ENZYMER01DK042303 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SMITH, JANET L. · 1990 to 2024
$6.6M
Molecular Analysis of Modular Polyketide SynthasesR01GM076477 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SHERMAN, DAVID H, SMITH, JANET L. · 2006 to 2018
$5.2M
GLUTAMINE AMIDOTRANSFERASES AND PARTNER ENZYMESR37DK042303 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SMITH, JANET L. · 1998 to 2007
$2.4M
Architectural Basis of Leptin Transmembrane SignalingR01DK090165 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SKINIOTIS, GEORGIOS · 2011 to 2017
$2.3M
Structural Basis of Substrate Processing in Modular Polyketide SynthasesR01GM115601 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SKINIOTIS, GEORGIOS · 2015 to 2018
$1.6M
NIDDK NIH HHS DK042303NIDDK NIH HHS DK090165NIDDK NIH HHS R01 DK042303NIDDK NIH HHS R01 DK090165NIDDK NIH HHS R37 DK042303NIGMS NIH HHS GM076477NIGMS NIH HHS R01 GM076477NIGMS NIH HHS R01 GM115601
6 · The paper itself

Abstract

Modular polyketide synthases (PKS) produce a vast array of bioactive molecules that are the basis of many highly valued pharmaceuticals. The biosynthesis of these compounds is based on ordered assembly lines of multi-domain modules, each extending and modifying a specific chain-elongation intermediate before transfer to the next module for further processing. The first 3D structures of a full polyketide synthase module in different functional states were obtained recently by electron cryo-microscopy. The unexpected module architecture revealed a striking evolutionary divergence of the polyketide synthase compared to its metazoan fatty acid synthase homolog, as well as remarkable conformational rearrangements dependent on its biochemical state during the full catalytic cycle. The design and dynamics of the module are highly optimized for both catalysis and fidelity in the construction of complex, biologically active natural products.

Indexed as

Acyl Carrier ProteinAnimalsCryoelectron MicroscopyEvolution, MolecularHumansPolyketide SynthasesProtein Structure, TertiaryAcyl Carrier ProteinPolyketide Synthases

Identifiers

PMID25791608
PMCPMC4476912
OpenAlexW2005357361

What OpenQuestion holds

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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.