Evidence map›Paper›PMID 32066964›Full record

ArticleNature structural & molecular biology2020

The structure of the cohesin ATPase elucidates the mechanism of SMC-kleisin ring opening.

Kyle W Muir, Yan Li, Felix Weis, Daniel Panne

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. NIPBL and STAG1 enable loop extrusion by providing differential DNA-cohesin affinity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Cohesin ring gates are specialized for meiotic cell division.Journal of molecular cell biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Molecular mechanism and functional significance of Wapl interaction with the Cohesin complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Article
  13. Structural biology of SMC complexes across the tree of life.Current opinion in structural biology · 2023
    Review
  14. DNA segment capture by Smc5/6 holocomplexes.Nature structural & molecular biology · 2023
    Article
  15. Article
  16. Review
  17. Article
  18. Clamping of DNA shuts the condensin neck gate.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. SMC complexes: Lifting the lid on loop extrusion.Current opinion in cell biology · 2022
    Review
  20. 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

4 authors at 4 institutions in 3 countries.

Kyle W MuirEuropean Molecular Biology Laboratory, Grenoble, France. kmuir@mrc-lmb.cam.ac.uk.ORCID http://orcid.org/0000-0002-0294-5679
Yan LiEuropean Molecular Biology Laboratory, Grenoble, France.
Felix WeisEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Daniel PanneEuropean Molecular Biology Laboratory, Grenoble, France. daniel.panne@leicester.ac.uk.ORCID http://orcid.org/0000-0001-9158-5507
European Molecular Biology Laboratory · DEEuropean Molecular Biology Laboratory · FRMRC Laboratory of Molecular Biology · GBUniversity of Leicester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Genome regulation requires control of chromosome organization by SMC-kleisin complexes. The cohesin complex contains the Smc1 and Smc3 subunits that associate with the kleisin Scc1 to form a ring-shaped complex that can topologically engage chromatin to regulate chromatin structure. Release from chromatin involves opening of the ring at the Smc3-Scc1 interface in a reaction that is controlled by acetylation and engagement of the Smc ATPase head domains. To understand the underlying molecular mechanisms, we have determined the 3.2-Å resolution cryo-electron microscopy structure of the ATPγS-bound, heterotrimeric cohesin ATPase head module and the 2.1-Å resolution crystal structure of a nucleotide-free Smc1-Scc1 subcomplex from Saccharomyces cerevisiae and Chaetomium thermophilium. We found that ATP-binding and Smc1-Smc3 heterodimerization promote conformational changes within the ATPase that are transmitted to the Smc coiled-coil domains. Remodeling of the coiled-coil domain of Smc3 abrogates the binding surface for Scc1, thus leading to ring opening at the Smc3-Scc1 interface.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAmino Acid SequenceBinding SitesCell Cycle ProteinsChaetomiumChromosomal Proteins, Non-HistoneCloning, MolecularCohesinsCryoelectron MicroscopyCrystallography, X-RayEscherichia coliGene ExpressionGenetic VectorsModels, MolecularProtein Bindingadenosine 5'-O-(3-thiotriphosphate)Adenosine TriphosphatasesAdenosine TriphosphateCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsMCD1 protein, S cerevisiaeRecombinant ProteinsSaccharomyces cerevisiae ProteinsSMC3 protein, S cerevisiaeStructural Maintenance of Chromosome Protein 1

Identifiers

PMID32066964
PMCPMC7100847
OpenAlexW3006529223

What OpenQuestion holds

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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.