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http://purl.uniprot.org/citations/7568114http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7568114http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7568114http://www.w3.org/2000/01/rdf-schema#comment"The crystal structure of the large fragment of the Thermus aquaticus DNA polymerase (Klentaq1), determined at 2.5-A resolution, demonstrates a compact two-domain architecture. The C-terminal domain is identical in fold to the equivalent region of the Klenow fragment of Escherichia coli DNA polymerase I (Klenow pol I). Although the N-terminal domain of Klentaq1 differs greatly in sequence from its counterpart in Klenow pol I, it has clearly evolved from a common ancestor. The structure of Klentaq1 reveals the strategy utilized by this protein to maintain activity at high temperatures and provides the structural basis for future improvements of the enzyme."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.org/dc/terms/identifier"doi:10.1073/pnas.92.20.9264"xsd:string
http://purl.uniprot.org/citations/7568114http://purl.org/dc/terms/identifier"doi:10.1073/pnas.92.20.9264"xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/author"Korolev S."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/author"Korolev S."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/author"Waksman G."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/author"Waksman G."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/author"Barnes W.M."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/author"Barnes W.M."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/author"Nayal M."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/author"Nayal M."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/author"di Cera E."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/author"di Cera E."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/pages"9264-9268"xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/pages"9264-9268"xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/title"Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-A resolution: structural basis for thermostability."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/title"Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-A resolution: structural basis for thermostability."xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/volume"92"xsd:string
http://purl.uniprot.org/citations/7568114http://purl.uniprot.org/core/volume"92"xsd:string