Evidence map›Paper›PMID 30659798›Full record

ArticleJournal of molecular biology2019

Cryo-EM Structure (4.5-Å) of Yeast Kinesin-5-Microtubule Complex Reveals a Distinct Binding Footprint and Mechanism of Drug Resistance.

Ottilie von Loeffelholz, Alejandro Peña, Douglas Robert Drummond, Robert Cross, Carolyn Ann Moores

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.2field-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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  4. Distinct regions of the kinesin-5 C-terminal tail are essential for mitotic spindle midzone localization and sliding force.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  7. Review
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  12. Hybrid method for representing ions in implicit solvation calculations.Computational and structural biotechnology journal · 2021
    Article
  13. These motors were made for walking.Protein science : a publication of the Protein Society · 2020
    Review
  14. Article
  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Ottilie von LoeffelholzInstitute of Structural and Molecular Biology, Birkbeck College, London, WC1E 7HX, UK.
Alejandro PeñaInstitute of Structural and Molecular Biology, Birkbeck College, London, WC1E 7HX, UK.
Douglas Robert DrummondDivision of Biomedical Cell Biology, Warwick Medical School, Coventry, CV4 7AL, UK.
Robert CrossDivision of Biomedical Cell Biology, Warwick Medical School, Coventry, CV4 7AL, UK.
Carolyn Ann MooresInstitute of Structural and Molecular Biology, Birkbeck College, London, WC1E 7HX, UK. Electronic address: c.moores@mail.cryst.bbk.ac.uk.
Institute of Structural and Molecular Biology · GBUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L00190X/1Biotechnology and Biological Sciences Research Council BB/L014211/1Wellcome TrustWellcome Trust 079605/Z/06/ZWellcome Trust 103895/Z/14/Z
6 · The paper itself

Abstract

Kinesin-5s are microtubule-dependent motors that drive spindle pole separation during mitosis. We used cryo-electron microscopy to determine the 4.5-Å resolution structure of the motor domain of the fission yeast kinesin-5 Cut7 bound to fission yeast microtubules and explored the topology of the motor-microtubule interface and the susceptibility of the complex to drug binding. Despite their non-canonical architecture and mechanochemistry, Schizosaccharomyces pombe microtubules were stabilized by epothilone at the taxane binding pocket. The overall Cut7 footprint on the S. pombe microtubule surface is altered compared to mammalian tubulin microtubules because of their different polymer architectures. However, the core motor-microtubule interaction is tightly conserved, reflected in similar Cut7 ATPase activities on each microtubule type. AMPPNP-bound Cut7 adopts a kinesin-conserved ATP-like conformation including cover neck bundle formation. However, the Cut7 ATPase is not blocked by a mammalian-specific kinesin-5 inhibitor, consistent with the non-conserved sequence and structure of its loop5 insertion.

Indexed as

Chromosome SegregationCryoelectron MicroscopyDrug ResistanceKinesinsMicrotubule-Associated ProteinsMicrotubulesMitosisProtein BindingSchizosaccharomycesSchizosaccharomyces pombe ProteinsSpindle ApparatusTubulinCut7 protein, S pombeKinesinsMicrotubule-Associated ProteinsSchizosaccharomyces pombe ProteinsTubulin3D reconstructionCut7cytoskeletonmitosismotor

Identifiers

PMID30659798
PMCPMC6378684
OpenAlexW2910539341

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.