Evidence map›Paper›PMID 31045565›Full record

ArticleActa crystallographica. Section F, Structural biology communications2019

Novel T9 loop conformation of filamenting temperature-sensitive mutant Z from Mycobacterium tuberculosis.

E O Lazo, J Jakoncic, S RoyChowdhury, D Awasthi, I Ojima

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2019. 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. Protein Architecture and Composition in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026
    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

5 authors.

E O LazoNational Synchrotron Light Source II, Brookhaven National Laboratory, Upton, New York, USA.
J JakoncicNational Synchrotron Light Source II, Brookhaven National Laboratory, Upton, New York, USA.
S RoyChowdhuryInstitute of Chemical Biology and Drug Discovery and Department of Chemistry, Stony Brook University, Stony Brook, NY 11794-3400, USA.
D AwasthiInstitute of Chemical Biology and Drug Discovery and Department of Chemistry, Stony Brook University, Stony Brook, NY 11794-3400, USA.
I OjimaInstitute of Chemical Biology and Drug Discovery and Department of Chemistry, Stony Brook University, Stony Brook, NY 11794-3400, USA.

Funding

X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN AP41RR012408 · NCRR · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI ORVILLE, ALLEN M · 1998 to 2011
$32.2M
Macromolecular Crystallography at the National Synchrotron Light SourceP41GM103473 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI SWEET, ROBERT M · 2012 to 2013
$4.9M
Novel Antimicrobials Targeting Cell DivisionR01AI078251 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI OJIMA, IWAO · 2009 to 2013
$1.9M
National Institute of Allergy and Infectious Diseases R01AI078251NCRR NIH HHS P41 RR012408NCRR NIH HHS P41RR012408NIAID NIH HHS R01 AI078251NIGMS NIH HHS GM-0080NIGMS NIH HHS P41 GM103473NIGMS NIH HHS P41GM103473NIGMS NIH HHS Y01 GM000080
6 · The paper itself

Abstract

As of 2017, tuberculosis had infected 1.7 billion people (23% of the population of the world) and caused ten million deaths. Mycobacterium tuberculosis (Mtb) is quickly evolving, and new strains are classified as multidrug resistant. Thus, the identification of novel druggable targets is essential to combat the proliferation of these drug-resistant strains. Filamenting temperature-sensitive mutant Z (FtsZ) is a key protein involved in cytokinesis, an important process for Mtb proliferation and viability. FtsZ is required for bacterial cell division because it polymerizes into a structure called the Z-ring, which recruits accessory division proteins to the septum. Here, the crystal structure of the MtbFtsZ protein has been determined to 3.46 Å resolution and is described as a dimer of trimers, with an inter-subunit interface between protomers AB and DE. In this work, a novel conformation of MtbFtsZ is revealed involving the T9 loop and the nucleotide-binding pocket of protomers BC and EF.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesCell DivisionCloning, MolecularCrystallography, X-RayCytoskeletal ProteinsEscherichia coliGene ExpressionGenetic VectorsKineticsModels, MolecularMutationMycobacterium tuberculosisProtein BindingProtein Conformation, alpha-HelicalBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaProtein SubunitsRecombinant Proteinsfilamenting temperature-sensitive mutant ZFtsZMycobacterium tuberculosisT9 looptuberculosis

Identifiers

PMID31045565
PMCPMC6497106

What OpenQuestion holds

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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.