4WSA

Crystal structure of Influenza B polymerase bound to the vRNA promoter (FluB1 form)

4WSA の概要

• エントリーDOI: 10.2210/pdb4wsa/pdb
• 分子名称: Influenza B vRNA promoter 3' end, Influenza B vRNA promoter 5' end, PA, ... (5 entities in total)
• 機能のキーワード: transferase-rna complex, transferase/rna
• 由来する生物種: Influenza B virus; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 273016.01

構造登録者

Reich, S.,Guilligay, D.,Pflug, A.,Cusack, S. (登録日: 2014-10-26, 公開日: 2014-11-19, 最終更新日: 2024-05-08)

主引用文献

Reich, S.,Guilligay, D.,Pflug, A.,Malet, H.,Berger, I.,Crepin, T.,Hart, D.,Lunardi, T.,Nanao, M.,Ruigrok, R.W.,Cusack, S.
Structural insight into cap-snatching and RNA synthesis by influenza polymerase.
Nature, 516:361-366, 2014

PubMed Abstract: Influenza virus polymerase uses a capped primer, derived by 'cap-snatching' from host pre-messenger RNA, to transcribe its RNA genome into mRNA and a stuttering mechanism to generate the poly(A) tail. By contrast, genome replication is unprimed and generates exact full-length copies of the template. Here we use crystal structures of bat influenza A and human influenza B polymerases (FluA and FluB), bound to the viral RNA promoter, to give mechanistic insight into these distinct processes. In the FluA structure, a loop analogous to the priming loop of flavivirus polymerases suggests that influenza could initiate unprimed template replication by a similar mechanism. Comparing the FluA and FluB structures suggests that cap-snatching involves in situ rotation of the PB2 cap-binding domain to direct the capped primer first towards the endonuclease and then into the polymerase active site. The polymerase probably undergoes considerable conformational changes to convert the observed pre-initiation state into the active initiation and elongation states.

PubMed: 25409151
DOI: 10.1038/nature14009

実験手法

X-RAY DIFFRACTION (3.4 Å)