6MII

Crystal structure of minichromosome maintenance protein MCM/DNA complex

6MII の概要

• エントリーDOI: 10.2210/pdb6mii/pdb
• 分子名称: Minichromosome maintenance protein MCM, DNA (5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3'), [[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-tris(fluoranyl)beryllium, ... (7 entities in total)
• 機能のキーワード: mcm, dna, helicase, aaa+, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 418753.61

構造登録者

Enemark, E.J.,Meagher, M.,Epling, L.B. (登録日: 2018-09-19, 公開日: 2019-07-24, 最終更新日: 2023-10-11)

主引用文献

Meagher, M.,Epling, L.B.,Enemark, E.J.
DNA translocation mechanism of the MCM complex and implications for replication initiation.
Nat Commun, 10:3117-3117, 2019

PubMed Abstract: The DNA translocation activity of the minichromosome maintenance (MCM) complex powers DNA strand separation of the replication forks of eukaryotes and archaea. Here we illustrate an atomic level mechanism for this activity with a crystal structure of an archaeal MCM hexamer bound to single-stranded DNA and nucleotide cofactors. Sequence conservation indicates this rotary mechanism is fully possible for all eukaryotes and archaea. The structure definitively demonstrates the ring orients during translocation with the N-terminal domain leading, indicating that the translocation activity could also provide the physical basis of replication initiation where a double-hexamer idly encircling double-stranded DNA transforms to single-hexamers that encircle only one strand. In this mechanism, each strand binds to the N-terminal tier of one hexamer and the AAA+ tier of the other hexamer such that one ring pulls on the other, aligning equivalent interfaces to enable each hexamer to pull its translocation strand outside of the opposing hexamer.

PubMed: 31308367
DOI: 10.1038/s41467-019-11074-3

実験手法

X-RAY DIFFRACTION (3.15 Å)