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3JA8

Cryo-EM structure of the MCM2-7 double hexamer

3JA8 の概要
エントリーDOI10.2210/pdb3ja8/pdb
EMDBエントリー6338
分子名称Minichromosome Maintenance 2, Minichromosome Maintenance 3, Minichromosome Maintenance 4, ... (7 entities in total)
機能のキーワードcryo-em, single particle, mcm2-7, dna replication, hydrolase
由来する生物種Saccharomyces cerevisiae S288c (yeast)
詳細
タンパク質・核酸の鎖数6
化学式量合計608932.45
構造登録者
Li, N.,Zhai, Y.,Zhang, Y.,Li, W.,Yang, M.,Lei, J.,Tye, B.K.,Gao, N. (登録日: 2015-05-09, 公開日: 2015-08-05, 最終更新日: 2024-03-20)
主引用文献Li, N.,Zhai, Y.,Zhang, Y.,Li, W.,Yang, M.,Lei, J.,Tye, B.K.,Gao, N.
Structure of the eukaryotic MCM complex at 3.8 angstrom
Nature, 524:186-191, 2015
Cited by
PubMed Abstract: DNA replication in eukaryotes is strictly regulated by several mechanisms. A central step in this replication is the assembly of the heterohexameric minichromosome maintenance (MCM2-7) helicase complex at replication origins during G1 phase as an inactive double hexamer. Here, using cryo-electron microscopy, we report a near-atomic structure of the MCM2-7 double hexamer purified from yeast G1 chromatin. Our structure shows that two single hexamers, arranged in a tilted and twisted fashion through interdigitated amino-terminal domain interactions, form a kinked central channel. Four constricted rings consisting of conserved interior β-hairpins from the two single hexamers create a narrow passageway that tightly fits duplex DNA. This narrow passageway, reinforced by the offset of the two single hexamers at the double hexamer interface, is flanked by two pairs of gate-forming subunits, MCM2 and MCM5. These unusual features of the twisted and tilted single hexamers suggest a concerted mechanism for the melting of origin DNA that requires structural deformation of the intervening DNA.
PubMed: 26222030
DOI: 10.1038/nature14685
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.8 Å)
構造検証レポート
Validation report summary of 3ja8
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-09に公開中

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