5LRP

Mopeia Virus Exonuclease domain complexed with Magnesium

5LRP の概要

• エントリーDOI: 10.2210/pdb5lrp/pdb
• 分子名称: Nucleoprotein, ZINC ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: mopeia virus, exonuclease magnesium, hydrolase
• 由来する生物種: Mopeia virus AN20410
• 細胞内の位置: Virion : Q5S581
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47305.46

構造登録者

Yekwa, E.L.,Khourieh, J.,Canard, B.,Ferron, F. (登録日: 2016-08-19, 公開日: 2017-07-05, 最終更新日: 2024-01-17)

主引用文献

Yekwa, E.,Khourieh, J.,Canard, B.,Papageorgiou, N.,Ferron, F.
Activity inhibition and crystal polymorphism induced by active-site metal swapping.
Acta Crystallogr D Struct Biol, 73:641-649, 2017

PubMed Abstract: The Arenaviridae family is one of the two RNA viral families that encode a 3'-5' exonuclease in their genome. An exonuclease domain is found in the Arenaviridae nucleoprotein and targets dsRNA specifically. This domain is directly involved in suppression of innate immunity in the host cell. Like most phosphate-processing enzymes, it requires a divalent metal ion such as Mg (or Mn) as a cofactor to catalyse nucleotide-cleavage and nucleotide-transfer reactions. On the other hand, calcium (Ca) inhibits this enzymatic activity, in spite of the fact that Mg and Ca present comparable binding affinities and biological availabilities. Here, the molecular and structural effects of the replacement of magnesium by calcium and its inhibition mechanism for phosphodiester cleavage, an essential reaction in the viral process of innate immunity suppression, are studied. Biochemical data and high-resolution structures of the Mopeia virus exonuclease domain complexed with each ion are reported for the first time. The consequences of the ion swap for the stability of the protein, the catalytic site and the functional role of a specific metal ion in enabling the catalytic cleavage of a dsRNA substrate are outlined.

PubMed: 28777079
DOI: 10.1107/S205979831700866X

実験手法

X-RAY DIFFRACTION (1.941 Å)