5HC1

Structure of EAV NSP11 H141A mutant at 3.10A

5HC1 の概要

• エントリーDOI: 10.2210/pdb5hc1/pdb
• 関連するPDBエントリー: 5HBZ
• 分子名称: Non-structural protein 11 (2 entities in total)
• 機能のキーワード: nsp11, equine arteritis virus, endoribonuclease, nonstructural protein 11, nidovirus, nf-kappab, hydrolase
• 由来する生物種: Equine arteritis virus Bucyrus (EAV)
• 細胞内の位置: Nsp1 papain-like cysteine proteinase: Host nucleus. Nsp2 cysteine proteinase: Host membrane ; Multi-pass membrane protein . Non-structural protein 3: Host membrane ; Multi-pass membrane protein . Non-structural protein 5-6-7: Host membrane ; Multi-pass membrane protein . 3C-like serine proteinase: Host cytoplasm . RNA-directed RNA polymerase: Host cytoplasm, host perinuclear region . Helicase: Host cytoplasm, host perinuclear region : P19811
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 97058.82

構造登録者

Zhang, M.F.,Chen, Z.Z. (登録日: 2016-01-04, 公開日: 2016-10-12, 最終更新日: 2023-11-08)

主引用文献

Zhang, M.,Li, X.,Deng, Z.,Chen, Z.,Liu, Y.,Gao, Y.,Wu, W.,Chen, Z.
Structural Biology of the Arterivirus nsp11 Endoribonucleases.
J. Virol., 91:-, 2017

PubMed Abstract: Endoribonuclease (NendoU) is unique and conserved as a major genetic marker in nidoviruses that infect vertebrate hosts. Arterivirus nonstructural protein 11 (nsp11) was shown to have NendoU activity and play essential roles in the viral life cycle. Here, we report three crystal structures of porcine reproductive and respiratory syndrome virus (PRRSV) and equine arteritis virus (EAV) nsp11 mutants. The structures of arterivirus nsp11 contain two conserved compact domains: the N-terminal domain (NTD) and C-terminal domain (CTD). The structures of PRRSV and EAV endoribonucleases are similar and conserved in the arterivirus, but they are greatly different from that of severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS) coronaviruses (CoV), representing important human pathogens in the Nidovirales order. The catalytic center of NendoU activity is located in the CTD, where a positively charged groove is next to the key catalytic residues conserved in nidoviruses. Although the NTD is nearly identical, the catalytic region of the arterivirus nsp11 family proteins is remarkably flexible, and the oligomerization may be concentration dependent. In summary, our structures provide new insight into this key multifunctional NendoU family of proteins and lay a foundation for better understanding of the molecular mechanism and antiviral drug development.

PubMed: 27795409
DOI: 10.1128/JVI.01309-16

実験手法

X-RAY DIFFRACTION (3.1 Å)