3DLR

Crystal structure of the catalytic core domain from PFV integrase

3DLR の概要

• エントリーDOI: 10.2210/pdb3dlr/pdb
• 関連するPDBエントリー: 1cxu
• 分子名称: Integrase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: retroviral integrase, rve superfamily domain, dna integration, dna recombination, endonuclease, hydrolase, magnesium, metal-binding, multifunctional enzyme, nuclease, nucleotidyltransferase, nucleus, transferase, virion
• 由来する生物種: Human spumaretrovirus (SFVcpz(hu))
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22670.94

構造登録者

Valkov, E.,Cherepanov, P. (登録日: 2008-06-29, 公開日: 2008-12-09, 最終更新日: 2024-10-30)

主引用文献

Valkov, E.,Gupta, S.S.,Hare, S.,Helander, A.,Roversi, P.,McClure, M.,Cherepanov, P.
Functional and structural characterization of the integrase from the prototype foamy virus.
Nucleic Acids Res., 37:243-255, 2009

PubMed Abstract: Establishment of the stable provirus is an essential step in retroviral replication, orchestrated by integrase (IN), a virus-derived enzyme. Until now, available structural information was limited to the INs of human immunodeficiency virus type 1 (HIV-1), avian sarcoma virus (ASV) and their close orthologs from the Lentivirus and Alpharetrovirus genera. Here, we characterized the in vitro activity of the prototype foamy virus (PFV) IN from the Spumavirus genus and determined the three-dimensional structure of its catalytic core domain (CCD). Recombinant PFV IN displayed robust and almost exclusively concerted integration activity in vitro utilizing donor DNA substrates as short as 16 bp, underscoring its significance as a model for detailed structural studies. Comparison of the HIV-1, ASV and PFV CCD structures highlighted both conserved as well as unique structural features such as organization of the active site and the putative host factor binding face. Despite possessing very limited sequence identity to its HIV counterpart, PFV IN was sensitive to HIV IN strand transfer inhibitors, suggesting that this class of inhibitors target the most conserved features of retroviral IN-DNA complexes.

PubMed: 19036793
DOI: 10.1093/nar/gkn938

実験手法

X-RAY DIFFRACTION (2.2 Å)