3O3H

T. maritima RNase H2 D107N in complex with nucleic acid substrate and manganese ions

3O3H の概要

• エントリーDOI: 10.2210/pdb3o3h/pdb
• 関連するPDBエントリー: 2etj 3O3F 3O3G
• 分子名称: Ribonuclease HII, DNA (5'-D(*GP*AP*AP*TP*CP*AP*GP*GP*TP*GP*TP*C)-3'), DNA/RNA (5'-D(*GP*AP*CP*AP*C)-R(P*C)-D(P*TP*GP*AP*TP*TP*C)-3'), ... (5 entities in total)
• 機能のキーワード: rnase h fold, nuclease, hydrolase-dna-rna hybrid complex, hydrolase/dna-rna hybrid
• 由来する生物種: Thermotoga maritima
• 細胞内の位置: Cytoplasm (Potential): Q9X017
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 32188.27

構造登録者

Rychlik, M.P.,Chon, H.,Cerritelli, S.M.,Klimek, P.,Crouch, R.J.,Nowotny, M. (登録日: 2010-07-24, 公開日: 2010-12-08, 最終更新日: 2024-02-21)

主引用文献

Rychlik, M.P.,Chon, H.,Cerritelli, S.M.,Klimek, P.,Crouch, R.J.,Nowotny, M.
Crystal Structures of RNase H2 in Complex with Nucleic Acid Reveal the Mechanism of RNA-DNA Junction Recognition and Cleavage.
Mol.Cell, 40:658-670, 2010

PubMed Abstract: Two classes of RNase H hydrolyze RNA of RNA/DNA hybrids. In contrast to RNase H1 that requires four ribonucleotides for cleavage, RNase H2 can nick duplex DNAs containing a single ribonucleotide, suggesting different in vivo substrates. We report here the crystal structures of a type 2 RNase H in complex with substrates containing a (5')RNA-DNA(3') junction. They revealed a unique mechanism of recognition and substrate-assisted cleavage. A conserved tyrosine residue distorts the nucleic acid at the junction, allowing the substrate to function in catalysis by participating in coordination of the active site metal ion. The biochemical and structural properties of RNase H2 explain the preference of the enzyme for junction substrates and establish the structural and mechanistic differences with RNase H1. Junction recognition is important for the removal of RNA embedded in DNA and may play an important role in DNA replication and repair.

PubMed: 21095591
DOI: 10.1016/j.molcel.2010.11.001

実験手法

X-RAY DIFFRACTION (2.8 Å)