5AMR

Structure of the La Crosse Bunyavirus polymerase in complex with the 3' viral RNA

5AMR の概要

• エントリーDOI: 10.2210/pdb5amr/pdb
• 関連するPDBエントリー: 5AMQ
• 分子名称: RNA POLYMERASE L, RNA, ... (4 entities in total)
• 機能のキーワード: hydrolase, polymerase, rnadrnapol, bunyavirus, rna
• 由来する生物種: BUNYAVIRUS LA CROSSE; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 270999.19

構造登録者

Reguera, J.,Gerlach, P.,Cusack, S. (登録日: 2015-03-12, 公開日: 2015-06-03, 最終更新日: 2024-05-08)

主引用文献

Gerlach, P.,Malet, H.,Cusack, S.,Reguera, J.
Structural Insights Into Bunyavirus Replication and its Regulation by the Vrna Promoter.
Cell(Cambridge,Mass.), 161:1267-, 2015

PubMed Abstract: Segmented negative-strand RNA virus (sNSV) polymerases transcribe and replicate the viral RNA (vRNA) within a ribonucleoprotein particle (RNP). We present cryo-EM and X-ray structures of, respectively, apo- and vRNA bound La Crosse orthobunyavirus (LACV) polymerase that give atomic-resolution insight into how such RNPs perform RNA synthesis. The complementary 3' and 5' vRNA extremities are sequence specifically bound in separate sites on the polymerase. The 5' end binds as a stem-loop, allosterically structuring functionally important polymerase active site loops. Identification of distinct template and product exit tunnels allows proposal of a detailed model for template-directed replication with minimal disruption to the circularised RNP. The similar overall architecture and vRNA binding of monomeric LACV to heterotrimeric influenza polymerase, despite high sequence divergence, suggests that all sNSV polymerases have a common evolutionary origin and mechanism of RNA synthesis. These results will aid development of replication inhibitors of diverse, serious human pathogenic viruses.

PubMed: 26004069
DOI: 10.1016/J.CELL.2015.05.006

実験手法

X-RAY DIFFRACTION (2.57 Å)