4PH3

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

4PH3 の概要

• エントリーDOI: 10.2210/pdb4ph3/pdb
• 分子名称: BLV capsid, IODIDE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: retroviral capsid ntd with no beta-hairpin, all alpha, viral protein
• 由来する生物種: Bovine leukemia virus (BLV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35012.47

構造登録者

Trajtenberg, F.,Obal, G.,Pritsch, O.,Buschiazzo, A. (登録日: 2014-05-03, 公開日: 2015-06-10, 最終更新日: 2024-11-20)

主引用文献

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

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: 26044299
DOI: 10.1126/science.aaa5182

実験手法

X-RAY DIFFRACTION (2.44 Å)