9E2Z

Cryo-EM structure of human CMG helicase stalled at G4-containing DNA template

これはPDB形式変換不可エントリーです。

9E2Z の概要

• エントリーDOI: 10.2210/pdb9e2z/pdb
• EMDBエントリー: 47473
• 分子名称: DNA replication licensing factor MCM2, DNA replication complex GINS protein SLD5, Cell division control protein 45 homolog, ... (19 entities in total)
• 機能のキーワード: helicase, dna replication, cell division, fork stalling, translocation, replication, replication-dna complex, replication/dna
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 738680.38

構造登録者

Allwein, B.,Batra, S.,Remus, D.,Hite, R. (登録日: 2024-10-23, 公開日: 2025-03-26)

主引用文献

Batra, S.,Allwein, B.,Kumar, C.,Devbhandari, S.,Bruning, J.G.,Bahng, S.,Lee, C.M.,Marians, K.J.,Hite, R.K.,Remus, D.
G-quadruplex-stalled eukaryotic replisome structure reveals helical inchworm DNA translocation.
Science, 387:eadt1978-eadt1978, 2025

PubMed Abstract: 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.

PubMed: 40048517
DOI: 10.1126/science.adt1978

実験手法

ELECTRON MICROSCOPY (2.6 Å)