Evidence map›Paper›PMID 41427673›Full record

ArticleProtein science : a publication of the Protein Society2026

Structural basis of product recognition by Mycobacterium tuberculosis fatty acid synthase.

Elnaz Khalili Samani, S M Naimul Hasan, Alexander F A Keszei, Mahtab Heydari, Mohammad T Mazhab-Jafari

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Structural basis of product recognition by Mycobacterium tuberculosis fatty acid synthase.Protein science : a publication of the Protein Society · 2026
    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.

Elnaz Khalili SamaniDepartment of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.
S M Naimul HasanDepartment of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.
Alexander F A KeszeiPrincess Margaret Cancer Center, University Health Network, Toronto, Ontario, Canada.
Mahtab HeydariPrincess Margaret Cancer Center, University Health Network, Toronto, Ontario, Canada.
Mohammad T Mazhab-JafariDepartment of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.ORCID https://orcid.org/0000-0003-0207-5877

Funding

CIHR 195698CIHR 419240Natural Sciences and Engineering Research Council of Canada RGPIN-2018-06070Ontario Graduate Scholarship awardPrincess Margaret Cancer Foundation
6 · The paper itself

Abstract

Microbial iterative fatty acid synthases (FAS) are versatile multienzymes under scrutiny for their potential as anti-infectious targets and their biotechnological applications. They produce saturated fatty acids with defined chain length and release them as coenzyme A-conjugates. How they recognize appropriate acyl length to initiate the process of product release is unknown. Here, we resolved two intermediate state structures of FAS, one from each of the two organisms: bacterium Mycobacterium tuberculosis and yeast Saccharomyces cerevisiae. These structures reveal how acyl carrier protein (ACP) domain and nascent fatty acids interact with the substrate-promiscuous malonyl-palmitoyl transferase (MPT) domain that is involved in product cleavage from the enzyme. MPT adopts a transient channel necessary for the accommodation of long-chain fatty acids. This channel is formed by the transient retraction of a conserved arginine side chain involved in malonate binding. These insights uncover structural determinants that enable M. tuberculosis type I FAS to produce very long-chain fatty acids used for evading host immunity in tuberculosis (TB).

Indexed as

Bacterial ProteinsFatty Acid SynthasesMycobacterium tuberculosisSaccharomyces cerevisiaeCrystallography, X-RayFatty AcidsModels, MolecularProtein DomainsBacterial ProteinsFatty AcidsFatty Acid SynthasescryoEMfatty acid synthasemycobacterium tuberculosisSaccharomyces cerevisiaestructural biology

Identifiers

PMID41427673
PMCPMC12720414

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.