Evidence map›Paper›PMID 24613487›Full record

ArticleStructure (London, England : 1993)2014

Lytic water dynamics reveal evolutionarily conserved mechanisms of ATP hydrolysis by TIP49 AAA+ ATPases.

Arina Afanasyeva, Angela Hirtreiter, Anne Schreiber, Dina Grohmann, Georgii Pobegalov, Adam R McKay, Irina Tsaneva, Michael Petukhov, Emmanuel Käs, Mikhail Grigoriev and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Molecular Mechanism of ATP Hydrolysis Catalyzed by p97: A QM/MM Study.Journal of chemical theory and computation · 2025
    Article
  2. Article
  3. ATP-Binding and Hydrolysis in Inflammasome Activation.Molecules (Basel, Switzerland) · 2020
    Review
  4. Article
  5. Structural evidence for the roles of divalent cations in actin polymerization and activation of ATP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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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

11 authors at 7 institutions in 4 countries.

Arina AfanasyevaDepartment of Biophysics, Saint Petersburg State Polytechnical University, Saint Petersburg 195251, Russia; Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, Gatchina 188300, Russia.
Angela HirtreiterDivision of Biosciences, Institute for Structural and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK.
Anne SchreiberDivision of Biosciences, Institute for Structural and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK.
Dina GrohmannPhysikalische und Theoretische Chemie - NanoBioSciences, Technische Universität Braunschweig, Braunschweig 38106, Germany.
Georgii PobegalovDepartment of Biophysics, Saint Petersburg State Polytechnical University, Saint Petersburg 195251, Russia.
Adam R McKayDepartment of Chemistry, University College London, London WC1H 0AJ, UK.
Irina TsanevaDivision of Biosciences, Institute for Structural and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK.
Michael PetukhovDepartment of Biophysics, Saint Petersburg State Polytechnical University, Saint Petersburg 195251, Russia; Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, Gatchina 188300, Russia.
Emmanuel KäsUMR 5099, CNRS, Toulouse F-31000, France; Laboratoire de Biologie Moléculaire Eucaryote, Université de Toulouse, Toulouse F-31000, France. Electronic address: kas@ibcg.biotoul.fr.
Mikhail GrigorievUMR 5099, CNRS, Toulouse F-31000, France; Laboratoire de Biologie Moléculaire Eucaryote, Université de Toulouse, Toulouse F-31000, France. Electronic address: grigor@biotoul.fr.
Finn WernerDivision of Biosciences, Institute for Structural and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK.
Institute of Structural and Molecular Biology · GBPetersburg Nuclear Physics Institute · RUUniversity College London · GBCentre National de la Recherche Scientifique · FRPeter the Great St. Petersburg Polytechnic University · RUTechnische Universität Braunschweig · DEUniversité Fédérale de Toulouse Midi-Pyrénées · FR

Funding

Biotechnology and Biological Sciences Research Council BB/E008232/1Biotechnology and Biological Sciences Research Council BB/H019332/1Wellcome Trust 079351/Z/06/ZWellcome Trust 096553
6 · The paper itself

Abstract

Eukaryotic TIP49a (Pontin) and TIP49b (Reptin) AAA+ ATPases play essential roles in key cellular processes. How their weak ATPase activity contributes to their important functions remains largely unknown and difficult to analyze because of the divergent properties of TIP49a and TIP49b proteins and of their homo- and hetero-oligomeric assemblies. To circumvent these complexities, we have analyzed the single ancient TIP49 ortholog found in the archaeon Methanopyrus kandleri (mkTIP49). All-atom homology modeling and molecular dynamics simulations validated by biochemical assays reveal highly conserved organizational principles and identify key residues for ATP hydrolysis. An unanticipated crosstalk between Walker B and Sensor I motifs impacts the dynamics of water molecules and highlights a critical role of trans-acting aspartates in the lytic water activation step that is essential for the associative mechanism of ATP hydrolysis.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateArchaeal ProteinsAspartic AcidBiological EvolutionConserved SequenceEscherichia coliEuryarchaeotaGene ExpressionHydrolysisMolecular Dynamics SimulationProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, SecondaryRecombinant ProteinsAdenosine TriphosphatasesAdenosine TriphosphateArchaeal ProteinsAspartic AcidRecombinant ProteinsWater

Identifiers

PMID24613487
PMCPMC3991330
OpenAlexW2154526685

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.