6G7E

Crystal structure of Chaetomium thermophilum Mot1 (E1434Q, 1837-1886 deletion mutant)

6G7E の概要

• エントリーDOI: 10.2210/pdb6g7e/pdb
• 分子名称: Helicase-like protein (1 entity in total)
• 機能のキーワード: atpase, hydrolase, transcription
• 由来する生物種: Chaetomium thermophilum var. thermophilum DSM 1495
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 209128.02

構造登録者

Butryn, A.,Hopfner, K.-P. (登録日: 2018-04-05, 公開日: 2018-10-17, 最終更新日: 2024-10-23)

主引用文献

Butryn, A.,Woike, S.,Shetty, S.J.,Auble, D.T.,Hopfner, K.P.
Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state.
Elife, 7:-, 2018

PubMed Abstract: Swi2/Snf2 ATPases remodel protein:DNA complexes in all of the fundamental chromosome-associated processes. The single-subunit remodeler Mot1 dissociates TATA box-binding protein (TBP):DNA complexes and provides a simple model for obtaining structural insights into the action of Swi2/Snf2 ATPases. Previously we reported how the N-terminal domain of Mot1 binds TBP, NC2 and DNA, but the location of the C-terminal ATPase domain remained unclear (Butryn et al., 2015). Here, we report the crystal structure of the near full-length Mot1 from Our data show that Mot1 adopts a ring like structure with a catalytically inactive resting state of the ATPase. Biochemical analysis suggests that TBP binding switches Mot1 into an ATP hydrolysis-competent conformation. Combined with our previous results, these data significantly improve the structural model for the complete Mot1:TBP:DNA complex and suggest a general mechanism for Mot1 action.

PubMed: 30289385
DOI: 10.7554/eLife.37774

実験手法

X-RAY DIFFRACTION (3.2129 Å)