Evidence map›Paper›PMID 23977156›Full record

ArticlePloS one2013

Functional mapping of human dynamin-1-like GTPase domain based on x-ray structure analyses.

Julia Wenger, Eva Klinglmayr, Chris Fröhlich, Clarissa Eibl, Ana Gimeno, Manuel Hessenberger, Sandra Puehringer, Oliver Daumke, Peter Goettig

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

57 citing papers in PubMed, 83 citations in OpenAlex.

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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

9 authors at 3 institutions in 2 countries.

Julia WengerDepartment of Molecular Biology, University of Salzburg, Salzburg, Austria.
Eva Klinglmayr
Chris Fröhlich
Clarissa Eibl
Ana Gimeno
Manuel Hessenberger
Sandra Puehringer
Oliver Daumke
Peter Goettig
University of Salzburg · ATMax Delbrück Center · DEFreie Universität Berlin · DE

Funding

Austrian Science Fund FWF J 3173
6 · The paper itself

Abstract

Human dynamin-1-like protein (DNM1L) is a GTP-driven molecular machine that segregates mitochondria and peroxisomes. To obtain insights into its catalytic mechanism, we determined crystal structures of a construct comprising the GTPase domain and the bundle signaling element (BSE) in the nucleotide-free and GTP-analogue-bound states. The GTPase domain of DNM1L is structurally related to that of dynamin and binds the nucleotide 5'-Guanylyl-imidodiphosphate (GMP-PNP) via five highly conserved motifs, whereas the BSE folds into a pocket at the opposite side. Based on these structures, the GTPase center was systematically mapped by alanine mutagenesis and kinetic measurements. Thus, residues essential for the GTPase reaction were characterized, among them Lys38, Ser39 and Ser40 in the phosphate binding loop, Thr59 from switch I, Asp146 and Gly149 from switch II, Lys216 and Asp218 in the G4 element, as well as Asn246 in the G5 element. Also, mutated Glu81 and Glu82 in the unique 16-residue insertion of DNM1L influence the activity significantly. Mutations of Gln34, Ser35, and Asp190 in the predicted assembly interface interfered with dimerization of the GTPase domain induced by a transition state analogue and led to a loss of the lipid-stimulated GTPase activity. Our data point to related catalytic mechanisms of DNM1L and dynamin involving dimerization of their GTPase domains.

Indexed as

Amino Acid SequenceCatalytic DomainCrystallography, X-RayDynaminsGTP PhosphohydrolasesGuanosine TriphosphateHumansHydrogen BondingHydrolysisKineticsMicrotubule-Associated ProteinsMitochondrial ProteinsModels, MolecularProtein BindingProtein MultimerizationProtein Structure, SecondaryDNM1L protein, humanDynaminsGTP PhosphohydrolasesGuanosine TriphosphateMicrotubule-Associated ProteinsMitochondrial Proteins

Identifiers

PMID23977156
PMCPMC3747075
OpenAlexW2088937171

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.