3TBK

Mouse RIG-I ATPase Domain

3TBK の概要

• エントリーDOI: 10.2210/pdb3tbk/pdb
• 分子名称: RIG-I Helicase Domain, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: dech helicase, helicase, atp binding, hydrolase
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cytoplasm : Q6Q899
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64038.47

構造登録者

Civril, F.,Bennett, M.D.,Hopfner, K.-P. (登録日: 2011-08-07, 公開日: 2011-10-26, 最終更新日: 2017-11-08)

主引用文献

Civril, F.,Bennett, M.,Moldt, M.,Deimling, T.,Witte, G.,Schiesser, S.,Carell, T.,Hopfner, K.P.
The RIG-I ATPase domain structure reveals insights into ATP-dependent antiviral signalling.
Embo Rep., 12:1127-1134, 2011

PubMed Abstract: RIG-I detects cytosolic viral dsRNA with 5' triphosphates (5'-ppp-dsRNA), thereby initiating an antiviral innate immune response. Here we report the crystal structure of superfamily 2 (SF2) ATPase domain of RIG-I in complex with a nucleotide analogue. RIG-I SF2 comprises two RecA-like domains 1A and 2A and a helical insertion domain 2B, which together form a 'C'-shaped structure. Domains 1A and 2A are maintained in a 'signal-off' state with an inactive ATP hydrolysis site by an intriguing helical arm. By mutational analysis, we show surface motifs that are critical for dsRNA-stimulated ATPase activity, indicating that dsRNA induces a structural movement that brings domains 1A and 2A/B together to form an active ATPase site. The structure also indicates that the regulatory domain is close to the end of the helical arm, where it is well positioned to recruit 5'-ppp-dsRNA to the SF2 domain. Overall, our results indicate that the activation of RIG-I occurs through an RNA- and ATP-driven structural switch in the SF2 domain.

PubMed: 21979817
DOI: 10.1038/embor.2011.190

実験手法

X-RAY DIFFRACTION (2.14 Å)