4ph3

N-terminal domain of the capsid protein from bovine leukaemia virus (with no beta-hairpin)

spinqualitylabelsall models 4ph3, resolution 2.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ph3 is a 2 chain structure with sequence from Bovine leukemia virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.44Å Ligands: CSO, GOL, IOD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function L0PI28_BLV Publication Abstract from PubMed Retroviruses depend upon 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 significantly from 6-fold symmetry, yet adjust to make two-dimensional pseudo-hexagonal 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. Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography.,Obal G, Trajtenberg F, Carrion F, Tome L, Larrieux N, Zhang X, Pritsch O, Buschiazzo A Science. 2015 Jun 4. pii: aaa5182. PMID:26044299 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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