9IKC

Orf virus scaffolding protein Orfv075

9IKC の概要

• エントリーDOI: 10.2210/pdb9ikc/pdb
• EMDBエントリー: 60655
• 分子名称: 62 kDa protein (2 entities in total)
• 機能のキーワード: scaffold protein, capsid protein, poxvirus, viral protein
• 由来する生物種: Orf virus (strain NZ2)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 190956.52

構造登録者

Hyun, J.,Kim, S.,Ko, S.,Kim, M.,Jang, Y. (登録日: 2024-06-27, 公開日: 2024-08-07)

主引用文献

Kim, S.,Ko, S.,Kim, M.,Jang, Y.,Hyun, J.
Cryo-EM structure of orf virus scaffolding protein orfv075.
Biochem.Biophys.Res.Commun., 728:150334-150334, 2024

PubMed Abstract: Capsid-like poxvirus scaffold proteins self-assemble into semi-regular lattice that govern the formation of spherical immature virus particles. The scaffolding is a critical step in virus morphogenesis as exemplified by the drug rifampicin that impairs the recruitment of scaffold onto the viral membrane in vaccinia virus (VACV). Here we report cryo-electron microscopy structure of scaffolding protein Orfv075 of orf virus (ORFV) that causes smallpox-like diseases in sheep, goats and occasionally humans via zoonotic infection. We demonstrate that the regions that are involved in intertrimeric interactions for scaffold assembly are largely conserved in comparison to its VACV orthologue protein D13 whose intermediate assembly structures have been previously characterized. By contrast, less conserved regions are located away from these interfaces, indicating both viruses share similar assembly mechanisms. We also show that the phenylalanine-rich binding site of rifampicin in D13 is conserved in Orfv075, and molecular docking simulation confirms similar binding modes. Our study provides structural basis of scaffolding protein as a target for anti-poxvirus treatment across wide range of poxvirus genera.

PubMed: 38968773
DOI: 10.1016/j.bbrc.2024.150334

実験手法

ELECTRON MICROSCOPY (1.9 Å)