5EYI

Structure of PRRSV apo-NSP11 at 2.16A

Summary for 5EYI

• Entry DOI: 10.2210/pdb5eyi/pdb
• Descriptor: Non-structural protein 11, SULFATE ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: non-structural protein 11, nsp11, beta interferon antagonist, endoribonuclease, hydrolase
• Biological source: PRRSV 16244B (Porcine reproductive and respiratory syndrome virus 16244B)
• Cellular location: Nsp1: Host nucleus . Nsp1-alpha papain-like cysteine proteinase: Host nucleus . Nsp1-beta papain-like cysteine proteinase: Host cytoplasm . 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 : Q9YN02
• Total number of polymer chains: 2
• Total formula weight: 50177.07

Authors

Zhang, M.F.,Chen, Z. (deposition date: 2015-11-25, release date: 2016-10-12, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.16 Å)