6FA9

CRYSTAL STRUCTURE OF THE DEAH-BOX HELICASE PRP2

6FA9 の概要

• エントリーDOI: 10.2210/pdb6fa9/pdb
• 分子名称: Putative mRNA splicing factor, SULFATE ION (3 entities in total)
• 機能のキーワード: splicing, atpase, helicase, g-patch, hydrolase
• 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: 73112.71

構造登録者

Schmitt, A.,Hamann, F.,Neumann, P.,Ficner, R. (登録日: 2017-12-15, 公開日: 2018-07-11, 最終更新日: 2024-01-17)

主引用文献

Schmitt, A.,Hamann, F.,Neumann, P.,Ficner, R.
Crystal structure of the spliceosomal DEAH-box ATPase Prp2.
Acta Crystallogr D Struct Biol, 74:643-654, 2018

PubMed Abstract: The DEAH-box ATPase Prp2 plays a key role in the activation of the spliceosome as it promotes the transition from the B to the catalytically active B* spliceosome. Here, four crystal structures of Prp2 are reported: one of the nucleotide-free state and three different structures of the ADP-bound state. The overall conformation of the helicase core, formed by two RecA-like domains, does not differ significantly between the ADP-bound and the nucleotide-free states. However, intrinsic flexibility of Prp2 is observed, varying the position of the C-terminal domains with respect to the RecA domains. Additionally, in one of the structures a unique ADP conformation is found which has not been observed in any other DEAH-box, DEAD-box or NS3/NPH-II helicase.

PubMed: 29968674
DOI: 10.1107/S2059798318006356

実験手法

X-RAY DIFFRACTION (2.6 Å)