5XF8

Cryo-EM structure of the Cdt1-MCM2-7 complex in AMPPNP state

「5H7I」から置き換えられました

5XF8 の概要

• エントリーDOI: 10.2210/pdb5xf8/pdb
• EMDBエントリー: 6671
• 分子名称: DNA replication licensing factor MCM2, DNA replication licensing factor MCM3, DNA replication licensing factor MCM4, ... (7 entities in total)
• 機能のキーワード: helicase, dna replication, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• 細胞内の位置: Nucleus: P29469 P24279 P30665 P29496 P53091; Cytoplasm : P38132 P47112
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 677976.49

構造登録者

Zhai, Y.,Cheng, E.,Wu, H.,Li, N.,Yung, P.Y.,Gao, N.,Tye, B.K. (登録日: 2017-04-09, 公開日: 2017-05-03, 最終更新日: 2025-03-12)

主引用文献

Zhai, Y.,Cheng, E.,Wu, H.,Li, N.,Yung, P.Y.,Gao, N.,Tye, B.K.
Open-ringed structure of the Cdt1-Mcm2-7 complex as a precursor of the MCM double hexamer
Nat. Struct. Mol. Biol., 24:300-308, 2017

PubMed Abstract: The minichromosome maintenance complex (MCM) hexameric complex (Mcm2-7) forms the core of the eukaryotic replicative helicase. During G1 phase, two Cdt1-Mcm2-7 heptamers are loaded onto each replication origin by the origin-recognition complex (ORC) and Cdc6 to form an inactive MCM double hexamer (DH), but the detailed loading mechanism remains unclear. Here we examine the structures of the yeast MCM hexamer and Cdt1-MCM heptamer from Saccharomyces cerevisiae. Both complexes form left-handed coil structures with a 10-15-Å gap between Mcm5 and Mcm2, and a central channel that is occluded by the C-terminal domain winged-helix motif of Mcm5. Cdt1 wraps around the N-terminal regions of Mcm2, Mcm6 and Mcm4 to stabilize the whole complex. The intrinsic coiled structures of the precursors provide insights into the DH formation, and suggest a spring-action model for the MCM during the initial origin melting and the subsequent DNA unwinding.

PubMed: 28191894
DOI: 10.1038/nsmb.3374

実験手法

ELECTRON MICROSCOPY (7.1 Å)