2MA3

NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Methanothermobacter thermautotrophicus

2MA3 の概要

• エントリーDOI: 10.2210/pdb2ma3/pdb
• NMR情報: BMRB: 19187
• 分子名称: DNA replication initiator (Cdc21/Cdc54) (1 entity in total)
• 機能のキーワード: minichromosome maintenance protein, mcm, winged helix, replication
• 由来する生物種: Methanothermobacter thermautotrophicus (Methanothermobacter thermautotrophicus)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10135.65

構造登録者

Wiedemann, C.,Ohlenschlager, O.,Medagli, B.,Onesti, S.,Gorlach, M. (登録日: 2013-06-26, 公開日: 2014-12-31, 最終更新日: 2024-05-15)

主引用文献

Wiedemann, C.,Szambowska, A.,Hafner, S.,Ohlenschlager, O.,Guhrs, K.H.,Gorlach, M.
Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex.
Nucleic Acids Res., 43:2958-2967, 2015

PubMed Abstract: The minichromosome maintenance complex (MCM) represents the replicative DNA helicase both in eukaryotes and archaea. Here, we describe the solution structure of the C-terminal domains of the archaeal MCMs of Sulfolobus solfataricus (Sso) and Methanothermobacter thermautotrophicus (Mth). Those domains consist of a structurally conserved truncated winged helix (WH) domain lacking the two typical 'wings' of canonical WH domains. A less conserved N-terminal extension links this WH module to the MCM AAA+ domain forming the ATPase center. In the Sso MCM this linker contains a short α-helical element. Using Sso MCM mutants, including chimeric constructs containing Mth C-terminal domain elements, we show that the ATPase and helicase activity of the Sso MCM is significantly modulated by the short α-helical linker element and by N-terminal residues of the first α-helix of the truncated WH module. Finally, based on our structural and functional data, we present a docking-derived model of the Sso MCM, which implies an allosteric control of the ATPase center by the C-terminal domain.

PubMed: 25712103
DOI: 10.1093/nar/gkv120

実験手法

SOLUTION NMR