Ontology highlight
ABSTRACT:
SUBMITTER: Muroya A
PROVIDER: S-EPMC2373963 | biostudies-literature | 2001 Apr
REPOSITORIES: biostudies-literature
Muroya A A Tsuchiya D D Ishikawa M M Haruki M M Morikawa M M Kanaya S S Morikawa K K
Protein science : a publication of the Protein Society 20010401 4
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 ...[more]