1IO2

Crystal structure of type 2 ribonuclease h from hyperthermophilic archaeon, thermococcus kodakaraensis kod1

1IO2 の概要

• エントリーDOI: 10.2210/pdb1io2/pdb
• 分子名称: RIBONUCLEASE HII (2 entities in total)
• 機能のキーワード: endonuclease, hydrolase
• 由来する生物種: Thermococcus kodakarensis
• 細胞内の位置: Cytoplasm (Potential): O74035
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23974.45

構造登録者

Muroya, A.,Tsuchiya, D.,Ishikawa, M.,Haruki, M.,Morikawa, M. (登録日: 2000-12-28, 公開日: 2001-04-18, 最終更新日: 2023-12-27)

主引用文献

Muroya, A.,Tsuchiya, D.,Ishikawa, M.,Haruki, M.,Morikawa, M.,Kanaya, S.,Morikawa, K.
Catalytic center of an archaeal type 2 ribonuclease H as revealed by X-ray crystallographic and mutational analyses.
Protein Sci., 10:707-714, 2001

PubMed Abstract: The catalytic center of an archaeal Type 2 RNase H has been identified by a combination of X-ray crystallographic and mutational analyses. The crystal structure of the Type 2 RNase H from Thermococcus kodakaraensis KOD1 has revealed that the N-terminal major domain adopts the RNase H fold, despite the poor sequence similarity to the Type 1 RNase H. Mutational analyses showed that the catalytic reaction requires four acidic residues, which are well conserved in the Type 1 RNase H and the members of the polynucleotidyl transferase family. Thus, the Type 1 and Type 2 RNases H seem to share a common catalytic mechanism, except for the requirement of histidine as a general base in the former enzyme. Combined with the results from deletion mutant analyses, the structure suggests that the C-terminal domain of the Type 2 RNase H is involved in the interaction with the DNA/RNA hybrid.

PubMed: 11274461
DOI: 10.1110/ps.48001

実験手法

X-RAY DIFFRACTION (2 Å)