3BSU

Hybrid-binding domain of human RNase H1 in complex with 12-mer RNA/DNA

3BSU の概要

• エントリーDOI: 10.2210/pdb3bsu/pdb
• 分子名称: RNA (5'-R(*GP*AP*CP*AP*CP*CP*UP*GP*AP*UP*UP*C)-3'), DNA (5'-D(*DGP*DAP*DAP*DTP*DCP*DAP*DGP*DGP*(5IU)P*DGP*DTP*DC)-3'), Ribonuclease H1, ... (5 entities in total)
• 機能のキーワード: rnase h, rna/dna hybrid, dsrna, hydrolase-rna-dna complex, hydrolase/rna/dna
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (Potential): O60930
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 52404.26

構造登録者

Nowotny, M.,Cerritelli, S.M.,Ghirlando, R.,Gaidamakov, S.A.,Crouch, R.J.,Yang, W. (登録日: 2007-12-26, 公開日: 2008-03-25, 最終更新日: 2024-02-21)

主引用文献

Nowotny, M.,Cerritelli, S.M.,Ghirlando, R.,Gaidamakov, S.A.,Crouch, R.J.,Yang, W.
Specific recognition of RNA/DNA hybrid and enhancement of human RNase H1 activity by HBD.
Embo J., 27:1172-1181, 2008

PubMed Abstract: Human RNase H1 contains an N-terminal domain known as dsRHbd for binding both dsRNA and RNA/DNA hybrid. We find that dsRHbd binds preferentially to RNA/DNA hybrids by over 25-fold and rename it as hybrid binding domain (HBD). The crystal structure of HBD complexed with a 12 bp RNA/DNA hybrid reveals that the RNA strand is recognized by a protein loop, which forms hydrogen bonds with the 2'-OH groups. The DNA interface is highly specific and contains polar residues that interact with the phosphate groups and an aromatic patch that appears selective for binding deoxyriboses. HBD is unique relative to non-sequence-specific dsDNA- and dsRNA-binding domains because it does not use positive dipoles of alpha-helices for nucleic acid binding. Characterization of full-length enzymes with defective HBDs indicates that this domain dramatically enhances both the specific activity and processivity of RNase H1. Similar activity enhancement by small substrate-binding domains linked to the catalytic domain likely occurs in other nucleic acid enzymes.

PubMed: 18337749
DOI: 10.1038/emboj.2008.44

実験手法

X-RAY DIFFRACTION (2.1 Å)