1BEV
BOVINE ENTEROVIRUS VG-5-27
Summary for 1BEV
| Entry DOI | 10.2210/pdb1bev/pdb |
| Descriptor | BOVINE ENTEROVIRUS COAT PROTEINS VP1 TO VP4, SULFATE ION, MYRISTIC ACID, ... (7 entities in total) |
| Functional Keywords | coat protein, bovine enterovirus vg-5-27, picornavirus, icosahedral virus, virus |
| Biological source | Bovine enterovirus (STRAIN VG-5-27) More |
| Cellular location | Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P12915 P12915 P12915 P12915 |
| Total number of polymer chains | 4 |
| Total formula weight | 92924.09 |
| Authors | Smyth, M.,Tate, J.,Lyons, C.,Hoey, E.,Martin, S.,Stuart, D. (deposition date: 1996-04-03, release date: 1998-09-16, Last modification date: 2024-02-07) |
| Primary citation | Smyth, M.,Tate, J.,Hoey, E.,Lyons, C.,Martin, S.,Stuart, D. Implications for viral uncoating from the structure of bovine enterovirus. Nat.Struct.Biol., 2:224-231, 1995 Cited by PubMed Abstract: We have determined the crystal structure of a bovine enterovirus, revealing that the topologies of the major capsid proteins and the overall architecture of the virion are similar to those of related picornaviruses. The external loops joining beta-strands are truncated and the canyon region is partially filled by an extension of the VP3 G-H loop giving the viral capsid a relatively smooth appearance. These changes may have implications for cell attachment. In spite of these differences the virus maintains a hydrophobic pocket within VP1, occupied by a specific 'pocket factor' which appears to be myristic acid. These observations support the proposal that a kinetic equilibrium exists between occupied and unoccupied pocket states, with occupation inhibiting uncoating. PubMed: 7773791DOI: 10.1038/nsb0395-224 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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