6QWS

Crystal structure of the Ski2 RNA-helicase Brr2 from Chaetomium thermophilum in the apo state

6QWS の概要

• エントリーDOI: 10.2210/pdb6qws/pdb
• 分子名称: Pre-mRNA splicing helicase-like protein, SULFATE ION (3 entities in total)
• 機能のキーワード: helicase brr2 ski2 chaetomium thermophilum splicing rna, rna binding protein
• 由来する生物種: Chaetomium thermophilum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 197018.75

構造登録者

Absmeier, E.,Santos, K.F.,Wahl, M.C. (登録日: 2019-03-06, 公開日: 2020-01-15, 最終更新日: 2024-01-24)

主引用文献

Absmeier, E.,Santos, K.F.,Wahl, M.C.
Molecular Mechanism Underlying Inhibition of Intrinsic ATPase Activity in a Ski2-like RNA Helicase.
Structure, 28:236-243.e3, 2020

PubMed Abstract: RNA-dependent NTPases can act as RNA/RNA-protein remodeling enzymes and typically exhibit low NTPase activity in the absence of RNA/RNA-protein substrates. How futile intrinsic NTP hydrolysis is prevented is frequently not known. The ATPase/RNA helicase Brr2 belongs to the Ski2-like family of nucleic acid-dependent NTPases and is an integral component of the spliceosome. Comprehensive nucleotide binding and hydrolysis studies are not available for a member of the Ski2-like family. We present crystal structures of Chaetomium thermophilum Brr2 in the apo, ADP-bound, and ATPγS-bound states, revealing nucleotide-induced conformational changes and a hitherto unknown ATPγS binding mode. Our results in conjunction with Brr2 structures in other molecular contexts reveal multiple molecular mechanisms that contribute to the inhibition of intrinsic ATPase activity, including an N-terminal region that restrains the RecA-like domains in an open conformation and exclusion of an attacking water molecule, and suggest how RNA substrate binding can lead to ATPase stimulation.

PubMed: 31859026
DOI: 10.1016/j.str.2019.11.014

実験手法

X-RAY DIFFRACTION (3.3 Å)