Evidence map›Paper›PMID 39794554›Full record

ArticleNature structural & molecular biology2025

Structure and catalytic mechanism of exogenous fatty acid recycling by AasS, a versatile acyl-ACP synthetase.

Haomin Huang, Chen Wang, Shenghai Chang, Tao Cui, Yongchang Xu, Man Huang, Huimin Zhang, Chun Zhou, Xing Zhang, Youjun Feng

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. RSC chemical biology · 2026
    Article
  4. bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. 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

10 authors.

Haomin Huang *Key Laboratory of Multiple Organ Failure (Ministry of Education), Departments of Microbiology and General Intensive Care Unit of the Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.ORCID http://orcid.org/0009-0000-6449-7165
Chen Wang *Department of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Shenghai Chang *Department of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Tao Cui *School of Life Sciences, Northwestern Polytechnical University, Xi'an, China.
Yongchang XuKey Laboratory of Multiple Organ Failure (Ministry of Education), Departments of Microbiology and General Intensive Care Unit of the Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Man HuangKey Laboratory of Multiple Organ Failure (Ministry of Education), Departments of Microbiology and General Intensive Care Unit of the Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Huimin ZhangCancer Center at Illinois, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Chun ZhouSchool of Public Health, Zhejiang University School of Medicine, Hangzhou, China. chunzhou@zju.edu.cn.ORCID http://orcid.org/0000-0002-9257-468X
Xing ZhangDepartment of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China. xzhang1999@zju.edu.cn.ORCID http://orcid.org/0000-0002-6776-326X
Youjun FengKey Laboratory of Multiple Organ Failure (Ministry of Education), Departments of Microbiology and General Intensive Care Unit of the Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China. fengyj@zju.edu.cn.ORCID http://orcid.org/0000-0001-8083-0175

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fatty acids (FAs) are essential building blocks for all the domains of life, of which bacterial de novo synthesis, called type II FA synthesis (FAS II), is energetically expensive. The recycling of exogenous FAs (eFAs) partially relieves the FAS II demand and, therefore, compromises the efficacy of FAS II-directed antimicrobials. The versatile acyl-acyl carrier protein (ACP) synthetase, AasS, enables bacterial channeling of diverse eFA nutrients through holo-ACP, an activated form of ACP. However, the molecular mechanism for AasS catalysis is not fully understood. Here we report a series of cryo-electron microscopy structures of AasS from the bioluminescent bacterium Vibrio harveyi to provide insights into the catalytic cycle. AasS forms a ring-shaped hexamer, with each protomer folding into two distinct domains. Biochemical and structural analysis suggests that AasS accommodates distinct eFA substrates and the conserved W230 residue has a gating role. Adenosine triphosphate and Mg

Indexed as

Bacterial ProteinsFatty AcidsVibrioAcyl Carrier ProteinAdenosine TriphosphateCryoelectron MicroscopyMagnesiumModels, MolecularProtein ConformationAcyl Carrier ProteinAdenosine TriphosphateBacterial ProteinsFatty AcidsMagnesium

Identifiers

PMID39794554
PMCPMC12086093

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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.