Catalytic center of an archaeal type 2 ribonuclease H as revealed by X-ray crystallographic and mutational analyses

被引:65
作者
Muroya, A
Tsuchiya, D
Ishikawa, M
Haruki, M
Morikawa, M
Kanaya, S
Morikawa, K
机构
[1] Biomol Engn Res Inst, Dept Biol Struct, Osaka 5650874, Japan
[2] Osaka Univ, Grad Sch Engn, Dept Mat & Life Sci, Osaka 5650871, Japan
关键词
ribonuclease H; DNA/RNA hybrid; polynucleotidyl transferase family; crystal structure; mutational analysis;
D O I
10.1110/ps.48001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:707 / 714
页数:8
相关论文
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