Evidence map›Paper›PMID 35137487›Full record

ArticleProtein science : a publication of the Protein Society2022

Solution structure and dynamics of the mitochondrial-targeted GTPase-activating protein (GAP) VopE by an integrated NMR/SAXS approach.

Kyle P Smith, Woonghee Lee, Marco Tonelli, Yeongjoon Lee, Samuel H Light, Gabriel Cornilescu, Srinivas Chakravarthy

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 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
0.4field-weighted citation impact, top 35% 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. 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

7 authors at 6 institutions in 1 country.

Kyle P SmithDepartment of Cell & Developmental Biology, Northwestern University Chicago, Illinois, USA.ORCID 0000-0003-0526-2176
Woonghee LeeDepartment of Chemistry, University of Colorado-Denver, Denver, Colorado, USA.ORCID 0000-0002-0964-203X
Marco TonelliNational Magnetic Resonance Facility at Madison, Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.
Yeongjoon LeeDepartment of Chemistry, University of Colorado-Denver, Denver, Colorado, USA.
Samuel H LightDepartment of Microbiology, University of Chicago, Chicago, Illinois, USA.
Gabriel CornilescuAdvanced Technology Research Facility, Frederick National Laboratory for Cancer Research, Leidos Biomedical Research, Inc., National Cancer Institute, National Institutes of Health, Frederick, Maryland, USA.
Srinivas ChakravarthyBiophysics Collaborative Access Team, Argonne National Laboratory, Argonne, Illinois, USA.
University of Denver · USArgonne National Laboratory · USLeidos (United States) · USNorthwestern University · USUniversity of Chicago · USUniversity of Wisconsin–Madison · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LEONIDAS C. PLATANIAS · 1993 to 2026
$153.9M
TRD3 NMRbox: Bayesian AnalyticsP41GM111135 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI HOCH, JEFFREY C · 2015 to 2024
$14.0M
TR&D 3: TECHNOLOGY DEVELOPMENT FOR NMR STUDIES OF SMALL MOLECULES (METABOLOMICS, NATURAL PRODUCTS, METABOLITE-PROTEIN INTERACTIONS) pp.537-585 P41GM103399 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2012 to 2019
$9.4M
900 MHz NMR Spectrometer Biomolecular InvestigationsP41GM066326 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN L · 2002 to 2006
$5.0M
Advanced Pixel Array Detector for Time-Resolved SAXS and Fiber DiffractionS10OD018090 · OD · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2014 to 2014
$529k
CONSOLE UPGRADES FOR NMR FACILITYS10RR008438 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1993 to 1993
–
NCI NIH HHS P30 CA060553NCRR NIH HHS S10 RR008438NIGMS NIH HHS P41 GM066326NIGMS NIH HHS P41 GM103399NIGMS NIH HHS P41 GM111135NIH HHS S10 OD018090
6 · The paper itself

Abstract

The bacterial pathogen Vibrio cholerae use a type III secretion system to inject effector proteins into a host cell. Recently, a putative Toxic GTPase Activating Protein (ToxGAP) called Vibrio outer protein E (VopE) was identified as a T3SS substrate and virulence factor that affected host mitochondrial dynamics and immune response. However, biophysical and structural characterization has been absent. Here, we describe solution NMR structure of the putative GTPase-activating protein (GAP) domain (73-204) of VopE. Using size exclusion chromatography coupled with small-angle x-ray scattering and residual dipolar coupling data, we restrained the MD process to efficiently determine the overall fold and improve the quality of the output calculated structures. Comparing the structure of VopE with other ToxGAP's revealed a similar overall fold with several features unique to VopE. Specifically, the "Bulge 1," α1 helix, and noteworthy "backside linker" elements on the N-terminus are dissimilar to the other ToxGAP's. By using NMR relaxation dispersion experiments, we demonstrate that these regions undergo motions on a > 6 s

Indexed as

GTPase-Activating ProteinsVibrioScattering, Small AngleVirulence FactorsX-Ray DiffractionGTPase-Activating ProteinsVirulence Factorscatalytic arginine fingerExoSGTP hydrolysishelical bundlemitochondrial dynamicsrelaxation dispersionsmall-angle x-ray scatteringT3SS secretion systemVibrio CholeraeYopE

Identifiers

PMID35137487
PMCPMC9047041
OpenAlexW4210925278

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.