1ZBF
Crystal structure of B. halodurans RNase H catalytic domain mutant D132N
1ZBF の概要
| エントリーDOI | 10.2210/pdb1zbf/pdb |
| 関連するPDBエントリー | 1zbi 1zbl |
| 分子名称 | ribonuclease H-related protein, SULFATE ION (3 entities in total) |
| 機能のキーワード | rnase h, rna/dna hybrid, dde motif, hydrolase |
| 由来する生物種 | Bacillus halodurans |
| 細胞内の位置 | Cytoplasm (Potential): Q9KEI9 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 16425.54 |
| 構造登録者 | Nowotny, M.,Gaidamakov, S.A.,Crouch, R.J.,Yang, W. (登録日: 2005-04-08, 公開日: 2005-07-12, 最終更新日: 2024-02-14) |
| 主引用文献 | Nowotny, M.,Gaidamakov, S.A.,Crouch, R.J.,Yang, W. Crystal Structures of RNase H Bound to an RNA/DNA Hybrid: Substrate Specificity and Metal-Dependent Catalysis. Cell(Cambridge,Mass.), 121:1005-1016, 2005 Cited by PubMed Abstract: RNase H belongs to a nucleotidyl-transferase superfamily, which includes transposase, retroviral integrase, Holliday junction resolvase, and RISC nuclease Argonaute. We report the crystal structures of RNase H complexed with an RNA/DNA hybrid and a mechanism for substrate recognition and two-metal-ion-dependent catalysis. RNase H specifically recognizes the A form RNA strand and the B form DNA strand. Structure comparisons lead us to predict the catalytic residues of Argonaute and conclude that two-metal-ion catalysis is a general feature of the superfamily. In nucleases, the two metal ions are asymmetrically coordinated and have distinct roles in activating the nucleophile and stabilizing the transition state. In transposases, they are symmetrically coordinated and exchange roles to alternately activate a water and a 3'-OH for successive strand cleavage and transfer by a ping-pong mechanism. PubMed: 15989951DOI: 10.1016/j.cell.2005.04.024 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.5 Å) |
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