2QY2

Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domainm.

2QY2 の概要

• エントリーDOI: 10.2210/pdb2qy2/pdb
• 関連するPDBエントリー: 2QZE 3BGY
• 分子名称: Probable mRNA-capping enzyme, ACETATE ION, CITRATE ANION, ... (4 entities in total)
• 機能のキーワード: mrna capping, phosphatase, beta tunnel, viral protein, hydrolase, mrna processing, multifunctional enzyme, nucleotidyltransferase, s-adenosyl-l-methionine, transferase
• 由来する生物種: Mimivirus
• 細胞内の位置: Virion: Q5UQX1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55601.94

構造登録者

Shuman, S.,Benarroch, D.,Smith, P. (登録日: 2007-08-13, 公開日: 2008-04-01, 最終更新日: 2024-02-21)

主引用文献

Benarroch, D.,Smith, P.,Shuman, S.
Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domain.
Structure, 16:501-512, 2008

PubMed Abstract: The RNA triphosphatase (RTPase) components of the mRNA capping apparatus are a bellwether of eukaryal taxonomy. Fungal and protozoal RTPases belong to the triphosphate tunnel metalloenzyme (TTM) family, exemplified by yeast Cet1. Several large DNA viruses encode metal-dependent RTPases unrelated to the cysteinyl-phosphatase RTPases of their metazoan host organisms. The origins of DNA virus RTPases are unclear because they are structurally uncharacterized. Mimivirus, a giant virus of amoeba, resembles poxviruses in having a trifunctional capping enzyme composed of a metal-dependent RTPase module fused to guanylyltransferase (GTase) and guanine-N7 methyltransferase domains. The crystal structure of mimivirus RTPase reveals a minimized tunnel fold and an active site strikingly similar to that of Cet1. Unlike homodimeric fungal RTPases, mimivirus RTPase is a monomer. The mimivirus TTM-type RTPase-GTase fusion resembles the capping enzymes of amoebae, providing evidence that the ancestral large DNA virus acquired its capping enzyme from a unicellular host.

PubMed: 18400173
DOI: 10.1016/j.str.2008.01.009

実験手法

X-RAY DIFFRACTION (2 Å)