1HRH

CRYSTAL STRUCTURE OF THE RIBONUCLEASE H DOMAIN OF HIV-1 REVERSE TRANSCRIPTASE

1HRH の概要

• エントリーDOI: 10.2210/pdb1hrh/pdb
• 分子名称: RIBONUCLEASE H (1 entity in total)
• 機能のキーワード: hydrolase(endoribonuclease)
• 由来する生物種: Human immunodeficiency virus 1
• 細胞内の位置: Gag-Pol polyprotein: Host cell membrane; Lipid-anchor. Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P03366
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30062.26

構造登録者

Davies /II, J.F.,Matthews, D.A. (登録日: 1991-03-06, 公開日: 1992-01-15, 最終更新日: 2024-02-07)

主引用文献

Davies 2nd., J.F.,Hostomska, Z.,Hostomsky, Z.,Jordan, S.R.,Matthews, D.A.
Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase.
Science, 252:88-95, 1991

PubMed Abstract: The crystal structure of the ribonuclease (RNase) H domain of HIV-1 reverse transcriptase (RT) has been determined at a resolution of 2.4 A and refined to a crystallographic R factor of 0.20. The protein folds into a five-stranded mixed beta sheet flanked by an asymmetric distribution of four alpha helices. Two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues. The overall structure is similar in most respects to the RNase H from Escherichia coli. Structural features characteristic of the retroviral protein suggest how it may interface with the DNA polymerase domain of p66 in the mature RT heterodimer. These features also offer insights into why the isolated RNase H domain is catalytically inactive but when combined in vitro with the isolated p51 domain of RT RNase H activity can be reconstituted. Surprisingly, the peptide bond cleaved by HIV-1 protease near the polymerase-RNase H junction of p66 is completely inaccessible to solvent in the structure reported here. This suggests that the homodimeric p66-p66 precursor of mature RT is asymmetric with one of the two RNase H domains at least partially unfolded.

PubMed: 1707186

実験手法

X-RAY DIFFRACTION (2.4 Å)