Evidence map›Paper›PMID 39865521›Full record

ArticleFEBS letters2025

Elucidation of interface interactions between a dehydratase domain and an acyl carrier protein in cremimycin polyketide synthase.

Kaede Kotagiri, Haruka Tachibana, Daisuke Kawasaki, Taichi Chisuga, Toma Kashima, Shinya Fushinobu, Fumitaka Kudo, Tadashi Eguchi, Akimasa Miyanaga

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

9 authors.

Kaede KotagiriDepartment of Chemistry, Tokyo Institute of Technology (Institute of Science Tokyo), Japan.
Haruka TachibanaGraduate School of Agricultural and Life Sciences, The University of Tokyo, Japan.
Daisuke KawasakiDepartment of Chemistry, Tokyo Institute of Technology (Institute of Science Tokyo), Japan.
Taichi ChisugaDepartment of Chemistry, Tokyo Institute of Technology (Institute of Science Tokyo), Japan.
Toma KashimaGraduate School of Agricultural and Life Sciences, The University of Tokyo, Japan.
Shinya FushinobuGraduate School of Agricultural and Life Sciences, The University of Tokyo, Japan.ORCID https://orcid.org/0000-0003-1346-6435
Fumitaka KudoDepartment of Chemistry, Tokyo Institute of Technology (Institute of Science Tokyo), Japan.
Tadashi EguchiDepartment of Chemistry, Tokyo Institute of Technology (Institute of Science Tokyo), Japan.
Akimasa MiyanagaDepartment of Chemistry, Tokyo Institute of Technology (Institute of Science Tokyo), Japan.ORCID https://orcid.org/0000-0003-2219-6051

Funding

Japan Society for the Promotion of Science 16H06451Japan Society for the Promotion of Science 20H02911Noda Institute for Scientific ResearchUehara Memorial Foundation
6 · The paper itself

Abstract

Modular polyketide synthases (PKSs) are multi-domain enzymes involved in the biosynthesis of polyketide natural products. The dehydratase (DH) domain catalyzes the dehydration of the β-hydroxyacyl unit attached to the acyl carrier protein (ACP) domain in modular PKS. Although the DH domain likely recognizes the cognate ACP domain during the dehydration reaction, the molecular basis of DH-ACP interactions remains elusive. In this study, we conducted cross-linking analysis using a pantetheine-type probe for investigating the ACP recognition of a fusion-DH protein generated from a split-DH domain of cremimycin PKS. Based on the AlphaFold 3-predicted model structure of the fusion-DH-ACP complex, DH-ACP interface residues were identified and validated by mutational analysis. Our findings provide the first detailed insights into domain-domain interactions between DH and ACP in modular PKSs.

Indexed as

Acyl Carrier ProteinBacterial ProteinsHydro-LyasesPolyketide SynthasesModels, MolecularProtein BindingProtein DomainsStreptomycesAcyl Carrier ProteinBacterial ProteinsHydro-LyasesPolyketide Synthasesacyl carrier proteincross‐linkingdehydratasedomain–domain interactionspolyketide synthase

Identifiers

PMID39865521
PMCPMC12035518

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.