Evidence map›Paper›PMID 36214571›Full record

ArticlemBio2022

GTP-Bound Escherichia coli FtsZ Filaments Are Composed of Tense Monomers: a Dynamic Nuclear Polarization-Nuclear Magnetic Resonance Study Using Interface Detection.

Kelsey M McCoy, Keith J Fritzsching, Ann E McDermott

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mBio, 2022. 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. 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

3 authors.

Kelsey M McCoyDepartment of Chemistry, Columbia Universitygrid.21729.3f, New York, New York, USA.ORCID 0000-0001-5389-6304
Keith J FritzschingDepartment of Chemistry, Columbia Universitygrid.21729.3f, New York, New York, USA.
Ann E McDermottDepartment of Chemistry, Columbia Universitygrid.21729.3f, New York, New York, USA.

Funding

TR&D4: Integrated pipeline for data analysisP41GM118302 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI PALMER, ARTHUR G · 2017 to 2021
$8.5M
RM1 Center on Macromolecular Dynamics by NMR Spectroscopy at the New York Structural Biology Center (CoMD/NMR)- Equipment Supplement RequestRM1GM145397 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI ARTHUR G PALMER · 2022 to 2026
$8.3M
Structural and Functional Studies of Potassium Channels by Solid State NMRR01GM088724 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI ANN E MCDERMOTT · 2009 to 2026
$5.6M
DYNAMIC NUCLEAR POLARIZATION SOLID STATE NMR SPECTROMETER FOR BIOMOLECULAR STUDIES10RR029249 · NCRR · NEW YORK STRUCTURAL BIOLOGY CENTER · PI MCDERMOTT, ANN E · 2010 to 2010
$2.3M
EXTRAMURAL RESEARCH FACILITIES CONSTRUCTIONC06RR015495 · NCRR · NEW YORK STRUCTURAL BIOLOGY CENTER · PI RIFKIND, RICHARD A · 2000 to 2000
$2.0M
NCRR NIH HHS C06 RR015495NCRR NIH HHS S10 RR029249NIGMS NIH HHS P41 GM118302NIGMS NIH HHS R01 GM088724NIGMS NIH HHS RM1 GM145397
6 · The paper itself

Abstract

FtsZ filaments are the major structural component of the bacterial Z ring and are drivers of bacterial division. Crystal structures for FtsZ from some Gram-positive bacteria in the presence of GTP analogs suggest the possibility of a high-energy, "tense" conformation. It remains important to elucidate whether this tense form is the dominant form in filaments. Using dynamic nuclear polarization (DNP) solid-state nuclear magnetic resonance (NMR) and differential isotopic labeling, we directly detected residues located at the intermonomer interface of GTP-bound wild-type (WT) Escherichia coli FtsZ filaments. We combined chemical shift prediction, homology modeling, and heteronuclear dipolar recoupling techniques to characterize the E. coli FtsZ filament interface and demonstrated that the monomers in active filaments assume a tense conformation.

Indexed as

Bacterial ProteinsEscherichia coliGuanosine TriphosphateMagnetic Resonance SpectroscopyStaphylococcus aureusBacterial ProteinsGuanosine TriphosphatecytoskeletonFtsZnuclear magnetic resonanceprotein-protein interactionsstructural biology

Identifiers

PMID36214571
PMCPMC9765660

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.