Crystal structure of the spliceosomal DEAH-box ATPase Prp2.

剪接体 DEAH - box ATPase Prp2 的晶体结构。

• 影响指数: 5.699
• 发表时间: Jul 2018 1
• 来源期刊: Acta Crystallogr D Struct Biol
• DOI: 10.1107/S2059798318006356
• PMID: 29968674
• 文章类型: Journal Article
• 作者列表: Schmitt A,Hamann F,Neumann P,Ficner R

关键词: DEAH-box; Prp2; RNA helicase; spliceosome

Mesh: Adenosine Diphosphate / chemistry; Chaetomium / chemistry; Crystallization; Crystallography, X-Ray; DEAD-box RNA Helicases / chemistry; Fungal Proteins / chemistry; Molecular Conformation; Protein Binding; Protein Conformation

Abstract

The DEAH-box ATPase Prp2 plays a key role in the activation of the spliceosome as it promotes the transition from the Bact 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.

摘要

DEAH-boxATPasePrp2在剪接体的激活中起关键作用，因为它促进了从Bact到催化活性B*剪接体的转变。这里,报道了Prp2的四种晶体结构:无核苷酸状态之一和ADP结合状态的三种不同结构。解旋酶核心的整体构象，由两个类似RecA的域组成，在ADP结合状态和无核苷酸状态之间没有显着差异。然而,观察到Prp2的内在柔韧性，改变C端结构域相对于RecA结构域的位置。此外,在其中一个结构中，发现了独特的ADP构象，在任何其他DEAH-box中均未观察到，DEAD-box或NS3/NPH-II解旋酶。