8QDJ

Ntaya virus methyltransferase in complex wih Sinefungin

8QDJ の概要

• エントリーDOI: 10.2210/pdb8qdj/pdb
• 分子名称: Ntaya virus methyltransferase, SINEFUNGIN, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: flavivirus, ntaya virus, sinefungin, methyltransferase, viral protein
• 由来する生物種: Ntaya virus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30045.39

構造登録者

Krejcova, K.,Boura, E.,Klima, M. (登録日: 2023-08-29, 公開日: 2024-09-04)

主引用文献

Krejcova, K.,Krafcikova, P.,Klima, M.,Chalupska, D.,Chalupsky, K.,Zilecka, E.,Boura, E.
Structural and functional insights in flavivirus NS5 proteins gained by the structure of Ntaya virus polymerase and methyltransferase.
Structure, 32:1099-1109.e3, 2024

PubMed Abstract: Flaviviruses are single-stranded positive-sense RNA (+RNA) viruses that are responsible for several (re)emerging diseases such as yellow, dengue, or West Nile fevers. The Zika epidemic highlighted their dangerousness when a relatively benign virus known since the 1950s turned into a deadly pathogen. The central protein for their replication is NS5 (non-structural protein 5), which is composed of the N-terminal methyltransferase (MTase) domain and the C-terminal RNA-dependent RNA-polymerase (RdRp) domain. It is responsible for both RNA replication and installation of the 5' RNA cap. We structurally and biochemically analyzed the Ntaya virus MTase and RdRp domains and we compared their properties to other flaviviral NS5s. The enzymatic centers are well conserved across Flaviviridae, suggesting that the development of drugs targeting all flaviviruses is feasible. However, the enzymatic activities of the isolated proteins were significantly different for the MTase domains.

PubMed: 38781970
DOI: 10.1016/j.str.2024.04.020

実験手法

X-RAY DIFFRACTION (1.8 Å)