5IZE

Hantaan virus L protein cap-snatching endonuclease

5IZE の概要

• エントリーDOI: 10.2210/pdb5ize/pdb
• 分子名称: RNA-directed RNA polymerase L, MANGANESE (III) ION (3 entities in total)
• 機能のキーワード: in complex with manganese metal ions, transferase
• 由来する生物種: Hantaan virus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41462.64

構造登録者

Reguera, J.,Cusack, S. (登録日: 2016-03-25, 公開日: 2016-06-29, 最終更新日: 2024-11-06)

主引用文献

Reguera, J.,Gerlach, P.,Rosenthal, M.,Gaudon, S.,Coscia, F.,Gunther, S.,Cusack, S.
Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases.
Plos Pathog., 12:e1005636-e1005636, 2016

PubMed Abstract: Segmented negative strand RNA viruses of the arena-, bunya- and orthomyxovirus families uniquely carry out viral mRNA transcription by the cap-snatching mechanism. This involves cleavage of host mRNAs close to their capped 5' end by an endonuclease (EN) domain located in the N-terminal region of the viral polymerase. We present the structure of the cap-snatching EN of Hantaan virus, a bunyavirus belonging to hantavirus genus. Hantaan EN has an active site configuration, including a metal co-ordinating histidine, and nuclease activity similar to the previously reported La Crosse virus and Influenza virus ENs (orthobunyavirus and orthomyxovirus respectively), but is more active in cleaving a double stranded RNA substrate. In contrast, Lassa arenavirus EN has only acidic metal co-ordinating residues. We present three high resolution structures of Lassa virus EN with different bound ion configurations and show in comparative biophysical and biochemical experiments with Hantaan, La Crosse and influenza ENs that the isolated Lassa EN is essentially inactive. The results are discussed in the light of EN activation mechanisms revealed by recent structures of full-length influenza virus polymerase.

PubMed: 27304209
DOI: 10.1371/journal.ppat.1005636

実験手法

X-RAY DIFFRACTION (1.7 Å)