[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleG-quadruplex-stalled eukaryotic replisome structure reveals helical inchworm DNA translocation.
Journal, issue, pagesScience, Vol. 387, Issue 6738, Page eadt1978, Year 2025
Publish dateMar 7, 2025
AuthorsSahil Batra / Benjamin Allwein / Charanya Kumar / Sujan Devbhandari / Jan-Gert Brüning / Soon Bahng / Chong M Lee / Kenneth J Marians / Richard K Hite / Dirk Remus /
PubMed AbstractDNA G-quadruplexes (G4s) are non-B-form DNA secondary structures that threaten genome stability by impeding DNA replication. To elucidate how G4s induce replication fork arrest, we characterized fork ...DNA G-quadruplexes (G4s) are non-B-form DNA secondary structures that threaten genome stability by impeding DNA replication. To elucidate how G4s induce replication fork arrest, we characterized fork collisions with preformed G4s in the parental DNA using reconstituted yeast and human replisomes. We demonstrate that a single G4 in the leading strand template is sufficient to stall replisomes by arresting the CMG helicase. Cryo-electron microscopy structures of stalled yeast and human CMG complexes reveal that the folded G4 is lodged inside the central CMG channel, arresting translocation. The G4 stabilizes the CMG at distinct translocation intermediates, suggesting an unprecedented helical inchworm mechanism for DNA translocation. These findings illuminate the eukaryotic replication fork mechanism under normal and perturbed conditions.
External linksScience / PubMed:40048517
MethodsEM (single particle)
Resolution2.41 - 4.3 Å
Structure data

EMDB-47470, PDB-9e2w:
Cryo-EM structure of yeast CMG helicase stalled at G4-containing DNA template, state 1
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-47471, PDB-9e2x:
Cryo-EM structure of yeast CMG helicase stalled at G4-containing DNA template, state 2
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-47472, PDB-9e2y:
Cryo-EM structure of yeast CMG helicase stalled at G4-containing DNA template, state 3
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-47473, PDB-9e2z:
Cryo-EM structure of human CMG helicase stalled at G4-containing DNA template
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-47747: C-tier local refinement of human CMG G4 stall state
Method: EM (single particle) / Resolution: 2.46 Å

EMDB-47748: N-tier local refinement of human CMG G4 stall state
Method: EM (single particle) / Resolution: 2.53 Å

EMDB-47749: Cdc45-GINS local refinement of human CMG G4 stall state
Method: EM (single particle) / Resolution: 2.41 Å

EMDB-47751: Yeast CMG-CTM G4 stall state 1 C-tier local refinement
Method: EM (single particle) / Resolution: 3.15 Å

EMDB-47753: Yeast CMG G4 stall state 1, N-tier local refinement
Method: EM (single particle) / Resolution: 3.06 Å

EMDB-47754: Yeast CMG G4 stall state 1 Cdc45-GINS local refinement
Method: EM (single particle) / Resolution: 3.12 Å

EMDB-47755: Yeast CMG G4 stall state 1 Tof1-Csm3 local refinement
Method: EM (single particle) / Resolution: 3.16 Å

EMDB-47757: C-tier local refinement of yeast CMG G4 stall state 2
Method: EM (single particle) / Resolution: 3.61 Å

EMDB-47758: N-tier local refinement of yeast CMG G4 stall state 2
Method: EM (single particle) / Resolution: 3.28 Å

EMDB-47759: Cdc45-GINS local refinement of yeast CMG G4 stall state 2
Method: EM (single particle) / Resolution: 3.45 Å

EMDB-47760: Tof1-Csm3 local refinement of yeast CMG G4 stall state 2
Method: EM (single particle) / Resolution: 4.3 Å

EMDB-47762: C-tier local refinement of yeast CMG G4 stall state 3
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-47763: N-tier focused refinement of yeast CMG G4 stall state 3
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-47764: Cdc45-GINS local refinement of yeast CMG G4 stall state 3
Method: EM (single particle) / Resolution: 3.11 Å

EMDB-47915: Consensus refinement of yeast CMG G4 stall state 2
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-47916: Consensus refinement of human CMG G4 stall state
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-47925: Consensus refinement of yeast CMG G4 stall state 1
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-47926: Consensus refinement of yeast CMG G4 stall state 3
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae w303 (yeast)
  • synthetic construct (others)
  • homo sapiens (human)
KeywordsREPLICATION/DNA / helicase / DNA replication / cell division / fork stalling / translocation / REPLICATION / REPLICATION-DNA complex

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more