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

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公開日
2001-04
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  • http://onlinelibrary.wiley.com/termsAndConditions#vor
DOI
  • 10.1110/ps.48001
公開者
Wiley

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<jats:title>Abstract</jats:title><jats:p>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 <jats:italic>Thermococcus kodakaraensis</jats:italic> 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.</jats:p>

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