4PH0
capsid protein from bovine leukemia virus
Summary for 4PH0
| Entry DOI | 10.2210/pdb4ph0/pdb |
| Descriptor | BLV capsid (1 entity in total) |
| Functional Keywords | retroviral capsid, all alpha, viral protein |
| Biological source | Bovine leukemia virus (BLV) |
| Total number of polymer chains | 6 |
| Total formula weight | 141621.75 |
| Authors | Trajtenberg, F.,Obal, G.,Pritsch, O.,Buschiazzo, A. (deposition date: 2014-05-03, release date: 2015-06-10, Last modification date: 2023-12-27) |
| Primary citation | Obal, G.,Trajtenberg, F.,Carrion, F.,Tome, L.,Larrieux, N.,Zhang, X.,Pritsch, O.,Buschiazzo, A. STRUCTURAL VIROLOGY. Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography. Science, 349:95-98, 2015 Cited by PubMed Abstract: Retroviruses depend on self-assembly of their capsid proteins (core particle) to yield infectious mature virions. Despite the essential role of the retroviral core, its high polymorphism has hindered high-resolution structural analyses. Here, we report the x-ray structure of the native capsid (CA) protein from bovine leukemia virus. CA is organized as hexamers that deviate substantially from sixfold symmetry, yet adjust to make two-dimensional pseudohexagonal arrays that mimic mature retroviral cores. Intra- and interhexameric quasi-equivalent contacts are uncovered, with flexible trimeric lateral contacts among hexamers, yet preserving very similar dimeric interfaces making the lattice. The conformation of each capsid subunit in the hexamer is therefore dictated by long-range interactions, revealing how the hexamers can also assemble into closed core particles, a relevant feature of retrovirus biology. PubMed: 26044299DOI: 10.1126/science.aaa5182 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7497 Å) |
Structure validation
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