9L2R
Crystal structure of the SeMet-derived C-terminal of viral responsive protein 15 (PmVRP15) from black tiger shrimp Penaeus monodon
Summary for 9L2R
| Entry DOI | 10.2210/pdb9l2r/pdb |
| Descriptor | Viral responsive protein, SULFATE ION (3 entities in total) |
| Functional Keywords | shrimp protein, viral responsive protein, white spot syndrome virus partner, unknown function |
| Biological source | Penaeus monodon (black tiger shrimp) |
| Total number of polymer chains | 3 |
| Total formula weight | 21962.92 |
| Authors | Laohawutthichai, P.,Kim, S.-Y.,Chek, M.F.,Krusong, K.,Hakoshima, T. (deposition date: 2024-12-17, release date: 2025-10-22) |
| Primary citation | Laohawutthichai, P.,Kim, S.Y.,Chek, M.F.,Jatuyosporn, T.,Tassanakajon, A.,Krusong, K.,Hakoshima, T. Structure of the C-terminal of Viral Responsive Protein 15 (VRP15): A Key Protein During White Spot Syndrome Virus (WSSV) Infection. J.Mol.Biol., 437:169329-169329, 2025 Cited by PubMed Abstract: White spot syndrome virus (WSSV) is a major serious threat to black tiger shrimp farming. WSSV infection induces a host protein, viral responsive protein 15 (VRP15), for viral assembly and nuclear egress. Here, we showed that the C-terminal tail of VRP15 (VRP15-C) interacts directly with the viral nucleocapsid tegument protein WSV399. The crystal structure of VRP15-C was determined at 1.5 Å. The structure showed that VRP15-C forms a dimer by forming an α-helix bundle structure and that the dimer further interacts with adjacent dimers to form a tetramer and a higher oligomer by intermolecular helix-helix interactions. The ability to form oligomeric forms may contribute to assembly of viral proteins to form a nucleocapsid of WSSV. PubMed: 40639753DOI: 10.1016/j.jmb.2025.169329 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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