5FMQ

Crystal structure of the mid, cap-binding, mid-link and 627 domains from avian influenza A virus polymerase PB2 subunit bound to M7GTP H32 crystal form

5FMQ の概要

• エントリーDOI: 10.2210/pdb5fmq/pdb
• 関連するPDBエントリー: 5FML 5FMM
• 分子名称: INFLUENZA A PB2 SUBUNIT, 7N-METHYL-8-HYDROGUANOSINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: viral protein, influenza a pb2-c region containing mid, cap-binding, mid- link, 627 and nls domains
• 由来する生物種: INFLUENZA A VIRUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55279.07

構造登録者

Thierry, E.,Pflug, A.,Hart, D.,Cusack, S. (登録日: 2015-11-07, 公開日: 2016-01-13, 最終更新日: 2024-01-10)

主引用文献

Thierry, E.,Guilligay, D.,Kosinski, J.,Bock, T.,Gaudon, S.,Round, A.,Pflug, A.,Hengrung, N.,El Omari, K.,Baudin, F.,Hart, D.J.,Beck, M.,Cusack, S.
Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of Pb2 Domains.
Mol.Cell, 61:125-, 2016

PubMed Abstract: Influenza virus polymerase transcribes or replicates the segmented RNA genome (vRNA) into respectively viral mRNA or full-length copies and initiates RNA synthesis by binding the conserved 3' and 5' vRNA ends (the promoter). In recent structures of promoter-bound polymerase, the cap-binding and endonuclease domains are configured for cap snatching, which generates capped transcription primers. Here, we present a FluB polymerase structure with a bound complementary cRNA 5' end that exhibits a major rearrangement of the subdomains within the C-terminal two-thirds of PB2 (PB2-C). Notably, the PB2 nuclear localization signal (NLS)-containing domain translocates ∼90 Å to bind to the endonuclease domain. FluA PB2-C alone and RNA-free FluC polymerase are similarly arranged. Biophysical and cap-dependent endonuclease assays show that in solution the polymerase explores different conformational distributions depending on which RNA is bound. The inherent flexibility of the polymerase allows it to adopt alternative conformations that are likely important during polymerase maturation into active progeny RNPs.

PubMed: 26711008
DOI: 10.1016/J.MOLCEL.2015.11.016

実験手法

X-RAY DIFFRACTION (3.1 Å)