4P37

Crystal structure of the Megavirus polyadenylate synthase

4P37 の概要

• エントリーDOI: 10.2210/pdb4p37/pdb
• 分子名称: Putative poly(A) polymerase catalytic subunit, DI(HYDROXYETHYL)ETHER, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (6 entities in total)
• 機能のキーワード: polya polymerase, transferase
• 由来する生物種: Megavirus chiliensis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 128743.97

構造登録者

Priet, S.,Lartigue, A.,Claverie, J.M.,Abergel, C. (登録日: 2014-03-06, 公開日: 2015-04-01, 最終更新日: 2024-11-20)

主引用文献

Priet, S.,Lartigue, A.,Debart, F.,Claverie, J.M.,Abergel, C.
mRNA maturation in giant viruses: variation on a theme.
Nucleic Acids Res., 43:3776-3788, 2015

PubMed Abstract: Giant viruses from the Mimiviridae family replicate entirely in their host cytoplasm where their genes are transcribed by a viral transcription apparatus. mRNA polyadenylation uniquely occurs at hairpin-forming palindromic sequences terminating viral transcripts. Here we show that a conserved gene cluster both encode the enzyme responsible for the hairpin cleavage and the viral polyA polymerases (vPAP). Unexpectedly, the vPAPs are homodimeric and uniquely self-processive. The vPAP backbone structures exhibit a symmetrical architecture with two subdomains sharing a nucleotidyltransferase topology, suggesting that vPAPs originate from an ancestral duplication. A Poxvirus processivity factor homologue encoded by Megavirus chilensis displays a conserved 5'-GpppA 2'O methyltransferase activity but is also able to internally methylate the mRNAs' polyA tails. These findings elucidate how the arm wrestling between hosts and their viruses to access the translation machinery is taking place in Mimiviridae.

PubMed: 25779049
DOI: 10.1093/nar/gkv224

実験手法

X-RAY DIFFRACTION (2.24 Å)