Evidence map›Paper›PMID 37314846›Full record

ArticleeLife2023

Integrative dynamic structural biology unveils conformers essential for the oligomerization of a large GTPase.

Thomas-O Peulen, Carola S Hengstenberg, Ralf Biehl, Mykola Dimura, Charlotte Lorenz, Alessandro Valeri, Julian Folz, Christian A Hanke, Semra Ince, Tobias Vöpel and 6 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. FAMP: A Software Framework for FRET-Based Integrative Modeling of RNA.Methods in molecular biology (Clifton, N.J.) · 2026
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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

16 authors at 5 institutions in 2 countries.

Thomas-O Peulen *Chair for Molecular Physical Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.ORCID 0000-0001-8478-9755
Carola S Hengstenberg *Physical Chemistry I, Ruhr University Bochum, Bochum, Germany.
Ralf BiehlJülich Centre for Neutron Science (JCNS-1) and Institute of Biological Information Processing (IBI-8), Forschungszentrum Jülich GmbH, Jülich, Germany.ORCID 0000-0002-1999-547X
Mykola DimuraChair for Molecular Physical Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.ORCID 0000-0002-9462-0264
Charlotte LorenzJülich Centre for Neutron Science (JCNS-1) and Institute of Biological Information Processing (IBI-8), Forschungszentrum Jülich GmbH, Jülich, Germany.ORCID 0000-0003-3614-341X
Alessandro ValeriChair for Molecular Physical Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Julian FolzChair for Molecular Physical Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Christian A HankeChair for Molecular Physical Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.ORCID 0000-0002-4826-4908
Semra IncePhysical Chemistry I, Ruhr University Bochum, Bochum, Germany.
Tobias VöpelPhysical Chemistry I, Ruhr University Bochum, Bochum, Germany.
Bela FaragoInstitut Laue-Langevin, Grenoble, France.
Holger GohlkeInstitut für Pharmazeutische und Medizinische Chemie, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.ORCID 0000-0001-8613-1447
Johann P KlareMacromolecular Structure Group, Department of Physics, University of Osnabrück, Osnabrück, Germany.ORCID 0000-0002-5761-5968
Andreas M StadlerJülich Centre for Neutron Science (JCNS-1) and Institute of Biological Information Processing (IBI-8), Forschungszentrum Jülich GmbH, Jülich, Germany.ORCID 0000-0003-2272-5232
Claus A M SeidelChair for Molecular Physical Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.ORCID 0000-0002-5171-149X
Christian HerrmannPhysical Chemistry I, Ruhr University Bochum, Bochum, Germany.
Heinrich Heine University Düsseldorf · DEForschungszentrum Jülich · DERuhr University Bochum · DEInstitut Laue-Langevin · FROsnabrück University · DE

Funding

European Research Council Advanced Grant 2014 hybridFRET (671208)
6 · The paper itself

Abstract

Guanylate binding proteins (GBPs) are soluble dynamin-like proteins that undergo a conformational transition for GTP-controlled oligomerization and disrupt membranes of intracellular parasites to exert their function as part of the innate immune system of mammalian cells. We apply neutron spin echo, X-ray scattering, fluorescence, and EPR spectroscopy as techniques for integrative dynamic structural biology to study the structural basis and mechanism of conformational transitions in the human GBP1 (hGBP1). We mapped hGBP1's essential dynamics from nanoseconds to milliseconds by motional spectra of sub-domains. We find a GTP-independent flexibility of the C-terminal effector domain in the µs-regime and resolve structures of two distinct conformers essential for an opening of hGBP1 like a pocket knife and for oligomerization. Our results on hGBP1's conformational heterogeneity and dynamics (intrinsic flexibility) deepen our molecular understanding relevant for its reversible oligomerization, GTP-triggered association of the GTPase-domains and assembly-dependent GTP-hydrolysis.

Indexed as

GTP-Binding ProteinsGTP PhosphohydrolasesAnimalsBiologyGuanosine TriphosphateHumansHydrolysisMammalsGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine Triphosphatecomputer simulationselectron paramagnetic resonancehumanlarge gtpasesmolecular biophysicsneutron spin-echo spectroscopysingle-molecule fluorescence spectroscopysmall-angle x-ray scatteringstructural biology

Identifiers

PMID37314846
PMCPMC10374282
OpenAlexW3016206591

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.