9IKC
Orf virus scaffolding protein Orfv075
Summary for 9IKC
| Entry DOI | 10.2210/pdb9ikc/pdb |
| EMDB information | 60655 |
| Descriptor | 62 kDa protein (2 entities in total) |
| Functional Keywords | scaffold protein, capsid protein, poxvirus, viral protein |
| Biological source | Orf virus (strain NZ2) |
| Total number of polymer chains | 3 |
| Total formula weight | 190956.52 |
| Authors | |
| Primary citation | 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 Cited by 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: 38968773DOI: 10.1016/j.bbrc.2024.150334 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.9 Å) |
Structure validation
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