1io2
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(New page: 200px<br /><applet load="1io2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1io2, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 15:24, 20 November 2007
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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. Active as Ribonuclease H, with EC number 3.1.26.4 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
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