3G29

Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: D179N mutant, neutral pH

3G29 の概要

• エントリーDOI: 10.2210/pdb3g29/pdb
• 関連するPDBエントリー: 3G0V 3G1G 3G1I 3G21 3G26 3G28
• 分子名称: Gag polyprotein (2 entities in total)
• 機能のキーワード: alpha-helical bundle, capsid protein, virion, viral protein, retrovirus
• 由来する生物種: Rous sarcoma virus (RSV-PrC)
• 細胞内の位置: Matrix protein p19: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p12: Virion (Potential): P03322
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16947.30

構造登録者

Kingston, R.L. (登録日: 2009-01-30, 公開日: 2009-06-02, 最終更新日: 2023-11-01)

主引用文献

Bailey, G.D.,Hyun, J.K.,Mitra, A.K.,Kingston, R.L.
Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly
Structure, 17:737-748, 2009

PubMed Abstract: In mature retroviral particles, the capsid protein (CA) forms a shell encasing the viral replication complex. Human immunodeficiency virus (HIV) CA dimerizes in solution, through its C-terminal domain (CTD), and this interaction is important for capsid assembly. In contrast, other retroviral capsid proteins, including that of Rous sarcoma virus (RSV), do not dimerize with measurable affinity. Here we show, using X-ray crystallography and other biophysical methods, that acidification causes RSV CA to dimerize in a fashion analogous to HIV CA, and that this drives capsid assembly in vitro. A pair of aspartic acid residues, located within the CTD dimer interface, explains why dimerization is linked to proton binding. Our results show that despite overarching structural similarities, the intermolecular forces responsible for forming and stabilizing the retroviral capsid differ markedly across retroviral genera. Our data further suggest that proton binding may regulate RSV capsid assembly, or modulate stability of the assembled capsid.

PubMed: 19446529
DOI: 10.1016/j.str.2009.03.010

実験手法

X-RAY DIFFRACTION (2.5 Å)