{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1362825894902073728.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1110/ps.48001"}},{"identifier":{"@type":"URI","@value":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.48001"}},{"identifier":{"@type":"URI","@value":"https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.48001"}},{"identifier":{"@type":"PMID","@value":"11274461"}},{"identifier":{"@type":"NAID","@value":"30018931946"}}],"dc:title":[{"@value":"Catalytic center of an archaeal type 2 ribonuclease H as revealed by X‐ray crystallographic and mutational analyses"}],"description":[{"type":"abstract","notation":[{"@value":"<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>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380861290923600004","@type":"Researcher","foaf:name":[{"@value":"Ayumu Muroya"}]},{"@id":"https://cir.nii.ac.jp/crid/1380861290923600003","@type":"Researcher","foaf:name":[{"@value":"Daisuke Tsuchiya"}]},{"@id":"https://cir.nii.ac.jp/crid/1380861290923600000","@type":"Researcher","foaf:name":[{"@value":"Momoyo Ishikawa"}]},{"@id":"https://cir.nii.ac.jp/crid/1380861290923600005","@type":"Researcher","foaf:name":[{"@value":"Mitsuru Haruki"}]},{"@id":"https://cir.nii.ac.jp/crid/1380861290923600002","@type":"Researcher","foaf:name":[{"@value":"Masaaki Morikawa"}]},{"@id":"https://cir.nii.ac.jp/crid/1380861290923600006","@type":"Researcher","foaf:name":[{"@value":"Shigenori Kanaya"}]},{"@id":"https://cir.nii.ac.jp/crid/1380861290923600001","@type":"Researcher","foaf:name":[{"@value":"Kosuke Morikawa"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"09618368"},{"@type":"EISSN","@value":"1469896X"}],"prism:publicationName":[{"@value":"Protein Science"}],"dc:publisher":[{"@value":"Wiley"}],"prism:publicationDate":"2001-04","prism:volume":"10","prism:number":"4","prism:startingPage":"707","prism:endingPage":"714"},"reviewed":"false","dcterms:accessRights":"http://purl.org/coar/access_right/c_abf2","dc:rights":["http://onlinelibrary.wiley.com/termsAndConditions#vor"],"url":[{"@id":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.48001"},{"@id":"https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.48001"}],"createdAt":"2002-07-27","modifiedAt":"2023-09-29","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Models,%20Molecular","dc:title":"Models, Molecular"},{"@id":"https://cir.nii.ac.jp/all?q=Ribonuclease%20H","dc:title":"Ribonuclease H"},{"@id":"https://cir.nii.ac.jp/all?q=Crystallography,%20X-Ray","dc:title":"Crystallography, X-Ray"},{"@id":"https://cir.nii.ac.jp/all?q=Archaea","dc:title":"Archaea"},{"@id":"https://cir.nii.ac.jp/all?q=Nucleotidyltransferases","dc:title":"Nucleotidyltransferases"},{"@id":"https://cir.nii.ac.jp/all?q=Substrate%20Specificity","dc:title":"Substrate Specificity"},{"@id":"https://cir.nii.ac.jp/all?q=Isoenzymes","dc:title":"Isoenzymes"},{"@id":"https://cir.nii.ac.jp/all?q=Thermococcus","dc:title":"Thermococcus"},{"@id":"https://cir.nii.ac.jp/all?q=Kinetics","dc:title":"Kinetics"},{"@id":"https://cir.nii.ac.jp/all?q=Catalytic%20Domain","dc:title":"Catalytic Domain"},{"@id":"https://cir.nii.ac.jp/all?q=Escherichia%20coli","dc:title":"Escherichia coli"},{"@id":"https://cir.nii.ac.jp/all?q=Mutagenesis,%20Site-Directed","dc:title":"Mutagenesis, Site-Directed"},{"@id":"https://cir.nii.ac.jp/all?q=Sequence%20Alignment","dc:title":"Sequence Alignment"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360004235723129216","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Structure and characterization of RNase H3 from <i>Aquifex aeolicus</i>"}]},{"@id":"https://cir.nii.ac.jp/crid/1360283694137135360","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Importance of an N-Terminal Extension in Ribonuclease HII from Bacillus stearothermophilus for Substrate Binding"}]},{"@id":"https://cir.nii.ac.jp/crid/1360285708138034688","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Slow Unfolding Pathway of Hyperthermophilic Tk-RNase H2 Examined by Pulse Proteolysis Using the Stable Protease 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