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1io2
From Proteopedia
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'''CRYSTAL STRUCTURE OF TYPE 2 RIBONUCLEASE H FROM HYPERTHERMOPHILIC ARCHAEON, THERMOCOCCUS KODAKARAENSIS KOD1''' | '''CRYSTAL STRUCTURE OF TYPE 2 RIBONUCLEASE H FROM HYPERTHERMOPHILIC ARCHAEON, THERMOCOCCUS KODAKARAENSIS KOD1''' | ||
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[[Category: Muroya, A.]] | [[Category: Muroya, A.]] | ||
[[Category: Tsuchiya, D.]] | [[Category: Tsuchiya, D.]] | ||
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Revision as of 17:12, 2 May 2008
CRYSTAL STRUCTURE OF TYPE 2 RIBONUCLEASE H FROM HYPERTHERMOPHILIC ARCHAEON, THERMOCOCCUS KODAKARAENSIS KOD1
Overview
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.
About this Structure
1IO2 is a Single protein structure of sequence from Thermococcus kodakarensis. Full crystallographic information is available from OCA.
Reference
Catalytic center of an archaeal type 2 ribonuclease H as revealed by X-ray crystallographic and mutational analyses., Muroya A, Tsuchiya D, Ishikawa M, Haruki M, Morikawa M, Kanaya S, Morikawa K, Protein Sci. 2001 Apr;10(4):707-14. PMID:11274461 Page seeded by OCA on Fri May 2 20:12:23 2008
