1IO2

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

Summary for 1IO2

• Entry DOI: 10.2210/pdb1io2/pdb
• Descriptor: RIBONUCLEASE HII (2 entities in total)
• Functional Keywords: endonuclease, hydrolase
• Biological source: Thermococcus kodakarensis
• Cellular location: Cytoplasm (Potential): O74035
• Total number of polymer chains: 1
• Total formula weight: 23974.45

Authors

Muroya, A.,Tsuchiya, D.,Ishikawa, M.,Haruki, M.,Morikawa, M. (deposition date: 2000-12-28, release date: 2001-04-18, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)