5HLJ
Crystal Structure of Major Envelope Protein VP24 from White Spot Syndrome Virus
Summary for 5HLJ
| Entry DOI | 10.2210/pdb5hlj/pdb |
| Descriptor | VP24 (2 entities in total) |
| Functional Keywords | wssv, vp24, envelope protein, viral protein |
| Biological source | White spot syndrome virus |
| Total number of polymer chains | 1 |
| Total formula weight | 21255.95 |
| Authors | Sun, L.F.,Su, Y.T.,Zhao, Y.H.,Fu, Z.Q.,Wu, Y.K. (deposition date: 2016-01-15, release date: 2016-09-14, Last modification date: 2024-04-03) |
| Primary citation | Sun, L.F.,Su, Y.T.,Zhao, Y.H.,Fu, Z.Q.,Wu, Y.K. Crystal Structure of Major Envelope Protein VP24 from White Spot Syndrome Virus Sci Rep, 6:32309-32309, 2016 Cited by PubMed Abstract: White spot syndrome virus (WSSV) is one of the major and most serious pathogen in the shrimp industry. As one of the most abundant envelope protein, VP24 acts as a core protein interacting with other structure proteins and plays an important role in virus assembly and infection. Here, we have presented the crystal structure of VP24 from WSSV. In the structure, VP24 consists of a nine-stranded β-barrel fold with mostly antiparallel β-strands, and the loops extending out the β-barrel at both N-terminus and C-terminus, which is distinct to those of the other two major envelope proteins VP28 and VP26. Structural comparison of VP24 with VP26 and VP28 reveals opposite electrostatic surface potential properties of them. These structural differences could provide insight into their differential functional mechanisms and roles for virus assembly and infection. Moreover, the structure reveals a trimeric assembly, suggesting a likely natural conformation of VP24 in viral envelope. Therefore, in addition to confirming the evolutionary relationship among the three abundant envelope proteins of WSSV, our structural studies also facilitate a better understanding of the molecular mechanism underlying special roles of VP24 in WSSV assembly and infection. PubMed: 27572278DOI: 10.1038/srep32309 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.406 Å) |
Structure validation
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