1PX5

Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase

1PX5 の概要

• エントリーDOI: 10.2210/pdb1px5/pdb
• 分子名称: 2'-5'-oligoadenylate synthetase 1, SULFATE ION (3 entities in total)
• 機能のキーワード: 5-stranded antiparalel beta sheet, four helix bundle, transferase
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Mitochondrion (By similarity): Q29599
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81223.12

構造登録者

Hartmann, R.,Justesen, J.,Sarkar, S.N.,Sen, G.C.,Yee, V.C. (登録日: 2003-07-02, 公開日: 2003-11-25, 最終更新日: 2025-03-26)

主引用文献

Hartmann, R.,Justesen, J.,Sarkar, S.N.,Sen, G.C.,Yee, V.C.
Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase
Mol.Cell, 12:1173-1185, 2003

PubMed Abstract: 2'-5'-oligoadenylate synthetases are interferon-induced, double-stranded RNA-activated antiviral enzymes which are the only proteins known to catalyze 2'-specific nucleotidyl transfer. This crystal structure of a 2'-5'-oligoadenylate synthetase reveals a structural conservation with the 3'-specific poly(A) polymerase that, coupled with structure-guided mutagenesis, supports a conserved catalytic mechanism for the 2'- and 3'-specific nucleotidyl transferases. Comparison with structures of other superfamily members indicates that the donor substrates are bound by conserved active site features while the acceptor substrates are oriented by nonconserved regions. The 2'-5'-oligoadenylate synthetases are activated by viral double-stranded RNA in infected cells and initiate a cellular response by synthesizing 2'-5'-oligoadenylates, which in turn activate RNase L. This crystal structure suggests that activation involves a domain-domain shift and identifies a putative dsRNA activation site that is probed by mutagenesis, thus providing structural insight into cellular recognition of viral double-stranded RNA.

PubMed: 14636576
DOI: 10.1016/S1097-2765(03)00433-7

実験手法

X-RAY DIFFRACTION (1.74 Å)