Evidence map›Paper›PMID 37860976›Full record

ArticleIUCrJ2023

Structural snapshots of Mycobacterium tuberculosis enolase reveal dual mode of 2PG binding and its implication in enzyme catalysis.

Mohammed Ahmad, Bhavya Jha, Sucharita Bose, Satish Tiwari, Abhisek Dwivedy, Deepshikha Kar, Ravikant Pal, Richard Mariadasse, Tanya Parish, Jeyaraman Jeyakanthan and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in IUCrJ, 2023. 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
0.3field-weighted citation impact, top 36% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. The allergenic potential of enolases: physiological and pathophysiological insights.Current opinion in allergy and clinical immunology · 2025
    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

12 authors at 6 institutions in 2 countries.

Mohammed AhmadStructural and Functional Biology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.ORCID 0000-0002-8467-7849
Bhavya JhaStructural and Functional Biology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.
Sucharita BoseInstitute for Stem Cell Science and Regenerative Medicine, Bangalore 560065, India.
Satish TiwariStructural and Functional Biology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.
Abhisek DwivedyStructural and Functional Biology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.
Deepshikha KarStructural and Functional Biology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.
Ravikant PalStructural and Functional Biology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.
Richard MariadasseDepartment of Bioinformatics, Alagappa University, Karaikudi, Tamil Nadu 630003, India.ORCID 0000-0002-3041-6993
Tanya ParishInfectious Disease Research Institute, 1616 Eastlake Avenue E, Suite 400, Seattle, WA 98102, USA.
Jeyaraman JeyakanthanDepartment of Bioinformatics, Alagappa University, Karaikudi, Tamil Nadu 630003, India.ORCID 0000-0002-4594-9610
Kutti R VinothkumarNational Centre for Biological Sciences, Tata Institute for Fundamental Research, Bangalore 560065, India.
Bichitra Kumar BiswalStructural and Functional Biology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.
National Institute of Immunology · INAlagappa University · INInfectious Disease Research Institute · USInstitute for Stem Cell Biology and Regenerative Medicine · INNational Centre for Biological Sciences · INPatliputra University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enolase, a ubiquitous enzyme, catalyzes the reversible conversion of 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the glycolytic pathway of organisms of all three domains of life. The underlying mechanism of the 2PG to PEP conversion has been studied in great detail in previous work, however that of the reverse reaction remains to be explored. Here we present structural snapshots of Mycobacterium tuberculosis (Mtb) enolase in apo, PEP-bound and two 2PG-bound forms as it catalyzes the conversion of PEP to 2PG. The two 2PG-bound complex structures differed in the conformation of the bound product (2PG) viz the widely reported canonical conformation and a novel binding pose, which we refer to here as the alternate conformation. Notably, we observed two major differences compared with the forward reaction: the presence of Mg

Indexed as

Mycobacterium tuberculosisPhosphopyruvate HydrataseCatalysisModels, MolecularProtein ConformationPhosphopyruvate Hydratasecryo-electron microscopyenolaseenzyme mechanismsgluconeogenesisMycobacterium tuberculosisX-ray crystallography

Identifiers

PMID37860976
PMCPMC10619443
OpenAlexW4387799374

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.