1VSF

ASV INTEGRASE CORE DOMAIN WITH MN(II) COFACTOR AND HEPES LIGAND, HIGH MG CONCENTRATION FORM

1VSF の概要

• エントリーDOI: 10.2210/pdb1vsf/pdb
• 分子名称: INTEGRASE, MANGANESE (II) ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: hydrolase, endonuclease, endoribonuclease
• 由来する生物種: Rous sarcoma virus (strain Schmidt-Ruppin)
• 細胞内の位置: Matrix protein p19: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p12: Virion (Potential): P03354
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17016.47

構造登録者

Bujacz, G.,Jaskolski, M.,Alexandratos, J.,Wlodawer, A. (登録日: 1995-11-29, 公開日: 1996-04-03, 最終更新日: 2024-02-14)

主引用文献

Bujacz, G.,Jaskolski, M.,Alexandratos, J.,Wlodawer, A.,Merkel, G.,Katz, R.A.,Skalka, A.M.
The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations.
Structure, 4:89-96, 1996

PubMed Abstract: Members of the structurally-related superfamily of enzymes that includes RNase H, RuvC resolvase, MuA transposase, and retroviral integrase require divalent cations for enzymatic activity. So far, cation positions are reported in the X-ray crystal structures of only two of these proteins, E. coli and human immunodeficiency virus 1 (HIV-1) RNase H. Details of the placement of metal ions in the active site of retroviral integrases are necessary for the understanding of the catalytic mechanism of these enzymes.

PubMed: 8805516
DOI: 10.1016/S0969-2126(96)00012-3

実験手法

X-RAY DIFFRACTION (2.05 Å)