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http://purl.uniprot.org/citations/17892305http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17892305http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17892305http://www.w3.org/2000/01/rdf-schema#comment"The crystal structure of ribonuclease HI from the hyperthermophilic archaeon Sulfolobus tokodaii (Sto-RNase HI) was determined at 1.6 A resolution. Sto-RNase HI exhibits not only RNase H activity but also double-stranded RNA-dependent ribonuclease (dsRNase) activity. The main-chain fold and steric configurations of the four acidic active-site residues of Sto-RNase HI are very similar to those of other type 1 RNases H. However, Arg118 of Sto-RNase HI is located at the position in which His124 of E. coli RNase HI, His539 of HIV-1 RNase H, and Glu188 of Bacillus halodurans RNase H are located. The mutation of this residue to Ala considerably reduced both the RNase H and dsRNase activities without seriously affecting substrate binding, suggesting that Arg118 is involved in catalytic function. This residue may promote product release by perturbing the coordination of the metal ion A as proposed for Glu188 of B. halodurans RNase H. In addition, the extreme C-terminal region of Sto-RNase HI is anchored to its core region by one disulfide bond and several hydrogen bonds. Differential scanning calorimetry measurements indicated that Sto-RNase HI is a hyperstable protein with a melting temperature of 102 degrees C. The mutations of the cysteine residues forming disulfide bond or elimination of the extreme C-terminal region greatly destabilized the protein, indicating that anchoring of the C-terminal tail is responsible for hyperstabilization of Sto-RNase HI."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.org/dc/terms/identifier"doi:10.1021/bi700830f"xsd:string
http://purl.uniprot.org/citations/17892305http://purl.org/dc/terms/identifier"doi:10.1021/bi700830f"xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/author"Koga Y."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/author"Koga Y."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/author"Kanaya S."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/author"Kanaya S."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/author"Takano K."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/author"Takano K."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/author"You D.J."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/author"You D.J."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/author"Chon H."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/author"Chon H."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/pages"11494-11503"xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/pages"11494-11503"xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/title"Crystal structure of type 1 ribonuclease H from hyperthermophilic archaeon Sulfolobus tokodaii: role of arginine 118 and C-terminal anchoring."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/title"Crystal structure of type 1 ribonuclease H from hyperthermophilic archaeon Sulfolobus tokodaii: role of arginine 118 and C-terminal anchoring."xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/volume"46"xsd:string
http://purl.uniprot.org/citations/17892305http://purl.uniprot.org/core/volume"46"xsd:string