Evidence map›Paper›PMID 27917833›Full record

ArticleActa crystallographica. Section F, Structural biology communications2016

Crystal structure of the toxin Msmeg_6760, the structural homolog of Mycobacterium tuberculosis Rv2035, a novel type II toxin involved in the hypoxic response.

R Alexandra Bajaj, Mark A Arbing, Annie Shin, Duilio Cascio, Linda Miallau

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Identification of Genes Encoded Toxin-Antitoxin System inInfectious disorders drug targets · 2024
    Article
  3. The Benefits of Toxicity:Microorganisms · 2023
    Article
  4. Small RNA MTS1338 Configures a Stress Resistance Signature inInternational journal of molecular sciences · 2023
    Article
  5. 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.

R Alexandra BajajUCLA-DOE Institute and Departments of Biological Chemistry and Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1570, USA.
Mark A ArbingUCLA-DOE Institute and Departments of Biological Chemistry and Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1570, USA.
Annie ShinUCLA-DOE Institute and Departments of Biological Chemistry and Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1570, USA.
Duilio CascioUCLA-DOE Institute and Departments of Biological Chemistry and Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1570, USA.
Linda MiallauUCLA-DOE Institute and Departments of Biological Chemistry and Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1570, USA.

Funding

Vulnerabilities in Mycobacterial Cell-Wall BiogenesisP01AI095208 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI ZHANG, JUNJIE · 2012 to 2022
$19.8M
NIAID NIH HHS P01 AI095208
6 · The paper itself

Abstract

The structure of Msmeg_6760, a protein of unknown function, has been determined. Biochemical and bioinformatics analyses determined that Msmeg_6760 interacts with a protein encoded in the same operon, Msmeg_6762, and predicted that the operon is a toxin-antitoxin (TA) system. Structural comparison of Msmeg_6760 with proteins of known function suggests that Msmeg_6760 binds a hydrophobic ligand in a buried cavity lined by large hydrophobic residues. Access to this cavity could be controlled by a gate-latch mechanism. The function of the Msmeg_6760 toxin is unknown, but structure-based predictions revealed that Msmeg_6760 and Msmeg_6762 are homologous to Rv2034 and Rv2035, a predicted novel TA system involved in Mycobacterium tuberculosis latency during macrophage infection. The Msmeg_6760 toxin fold has not been previously described for bacterial toxins and its unique structural features suggest that toxin activation is likely to be mediated by a novel mechanism.

Indexed as

Gene Expression Regulation, BacterialAmino Acid SequenceAntigens, BacterialAntitoxinsBacterial ProteinsBacterial ToxinsBinding SitesCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionModels, MolecularMycobacterium smegmatisMycobacterium tuberculosisOperonPlasmidsAntigens, BacterialAntitoxinsBacterial ProteinsBacterial ToxinsRecombinant ProteinsRepressor ProteinsRv2034 protein, Mycobacterium tuberculosisbacterial latencymacrophage infectionMycobacterium smegmatisMycobacterium tuberculosisnovel foldsprotein structuretoxin–antitoxin complexesX-ray crystallography

Identifiers

PMID27917833
PMCPMC5137462

What OpenQuestion holds

Textmetadata
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.