3O3H

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

Summary for 3O3H

• Entry DOI: 10.2210/pdb3o3h/pdb
• Related: 2etj 3O3F 3O3G
• Descriptor: 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)
• Functional Keywords: rnase h fold, nuclease, hydrolase-dna-rna hybrid complex, hydrolase/dna-rna hybrid
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm (Potential): Q9X017
• Total number of polymer chains: 3
• Total formula weight: 32188.27

Authors

Rychlik, M.P.,Chon, H.,Cerritelli, S.M.,Klimek, P.,Crouch, R.J.,Nowotny, M. (deposition date: 2010-07-24, release date: 2010-12-08, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)