Evidence map›Paper›PMID 28191893›Full record

ArticleNature structural & molecular biology2017

Structural basis of Mcm2-7 replicative helicase loading by ORC-Cdc6 and Cdt1.

Zuanning Yuan, Alberto Riera, Lin Bai, Jingchuan Sun, Saikat Nandi, Christos Spanos, Zhuo Angel Chen, Marta Barbon, Juri Rappsilber, Bruce Stillman and 2 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

112 citing papers in PubMed, 175 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A Meier-Gorlin syndrome mutation impairs the loading of the MCM2-7 complex during DNA replication initiation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. An Orc6 tether mediates ORC binding-site switching during replication origin licensing.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Compact Origins and Where to Find Them: ORC's Guide to Genome-Wide Licensing.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  15. Review
  16. Article
  17. DNA bending mediated by ORC is essential for replication licensing in budding yeast.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Review
  19. Article
  20. Article

52 more citing papers are in PubMed but not listed here.

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

12 authors at 4 institutions in 3 countries.

Zuanning YuanCryo-EM Structural Biology Laboratory, Van Andel Research Institute, Grand Rapids, Michigan, USA.
Alberto RieraMRC London Institute of Medical Sciences (LMS), London, UK.
Lin BaiCryo-EM Structural Biology Laboratory, Van Andel Research Institute, Grand Rapids, Michigan, USA.
Jingchuan SunCryo-EM Structural Biology Laboratory, Van Andel Research Institute, Grand Rapids, Michigan, USA.
Saikat NandiCold Spring Harbor Laboratory, Cold Spring Harbor, New York, USA.ORCID 0000-0002-5693-6129
Christos SpanosWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.
Zhuo Angel ChenWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.
Marta BarbonMRC London Institute of Medical Sciences (LMS), London, UK.
Juri RappsilberWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.ORCID 0000-0001-5999-1310
Bruce StillmanCold Spring Harbor Laboratory, Cold Spring Harbor, New York, USA.ORCID 0000-0002-9453-4091
Christian SpeckMRC London Institute of Medical Sciences (LMS), London, UK.ORCID 0000-0001-6646-1692
Huilin LiCryo-EM Structural Biology Laboratory, Van Andel Research Institute, Grand Rapids, Michigan, USA.
Van Andel Institute · USMRC London Institute of Medical Sciences · GBWellcome Centre for Cell Biology · GBCold Spring Harbor Laboratory · US

Funding

Single-Cell Biology Shared ResourceP30CA045508 · NCI · COLD SPRING HARBOR LABORATORY · PI John Edward Moses · 1987 to 2026
$118.9M
REGULATION OF DNA REPLICATIONR01GM045436 · NIGMS · COLD SPRING HARBOR LABORATORY · PI STILLMAN, BRUCE W. · 1991 to 2025
$15.8M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
Structural mechanism of DNA replicationR35GM131754 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI Huilin Li · 2019 to 2026
$6.0M
A 200KV CRYO-TEM FOR IMAGING BIOLOGICAL STRUCTURESS10OD012272 · OD · STATE UNIVERSITY NEW YORK STONY BROOK · PI NEIMAN, AARON M · 2015 to 2015
$2.0M
Structural Basis of Eukaryotic Replication Initiation by Cryo-EMR01GM111742 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI LI, HUILIN · 2015 to 2018
$1.4M
Biotechnology and Biological Sciences Research Council P56061Medical Research Council MC_U120085811NCI NIH HHS P30 CA045508NIGMS NIH HHS P41 GM103310NIGMS NIH HHS R01 GM045436NIGMS NIH HHS R01 GM111742NIGMS NIH HHS R35 GM131754NIH HHS S10 OD012272Wellcome Trust 092076Wellcome Trust 103139Wellcome Trust 103139/Z/13/ZWellcome Trust 107903Wellcome Trust 108504Wellcome Trust P56628
6 · The paper itself

Abstract

To initiate DNA replication, the origin recognition complex (ORC) and Cdc6 load an Mcm2-7 double hexamer onto DNA. Without ATP hydrolysis, ORC-Cdc6 recruits one Cdt1-bound Mcm2-7 hexamer, thus forming an ORC-Cdc6-Cdt1-Mcm2-7 (OCCM) helicase-loading intermediate. Here we report a 3.9-Å structure of Saccharomyces cerevisiae OCCM on DNA. Flexible Mcm2-7 winged-helix domains (WHDs) engage ORC-Cdc6. A three-domain Cdt1 configuration embraces Mcm2, Mcm4, and Mcm6, thus comprising nearly half of the hexamer. The Cdt1 C-terminal domain extends to the Mcm6 WHD, which binds the Orc4 WHD. DNA passes through the ORC-Cdc6 and Mcm2-7 rings. Origin DNA interaction is mediated by an α-helix within Orc4 and positively charged loops within Orc2 and Cdc6. The Mcm2-7 C-tier AAA+ ring is topologically closed by an Mcm5 loop that embraces Mcm2, but the N-tier-ring Mcm2-Mcm5 interface remains open. This structure suggests a loading mechanism of the first Cdt1-bound Mcm2-7 hexamer by ORC-Cdc6.

Indexed as

DNA ReplicationReplication OriginBinding SitesCell Cycle ProteinsCryoelectron MicroscopyDNA-Binding ProteinsDNA, FungalMass SpectrometryMinichromosome Maintenance ProteinsModels, MolecularNucleotidesProtein BindingProtein DomainsProtein MultimerizationProtein Structure, SecondarySaccharomyces cerevisiaeCDC6 protein, S cerevisiaeCell Cycle ProteinsDNA-Binding ProteinsDNA, FungalMinichromosome Maintenance ProteinsNucleotidesSaccharomyces cerevisiae ProteinsTAH11 protein, S cerevisiae

Identifiers

PMID28191893
PMCPMC5503505
OpenAlexW2588958371

What OpenQuestion holds

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LicenceTDM
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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.