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http://purl.uniprot.org/citations/14592988http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14592988http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14592988http://www.w3.org/2000/01/rdf-schema#comment"CCA-adding enzyme [ATP(CTP):tRNA nucleotidyltransferase], a template-independent RNA polymerase, adds the defined 'cytidine-cytidine-adenosine' sequence onto the 3' end of tRNA. The archaeal CCA-adding enzyme (class I) and eubacterial/eukaryotic CCA-adding enzyme (class II) show little amino acid sequence homology, but catalyze the same reaction in a defined fashion. Here, we present the crystal structures of the class I archaeal CCA-adding enzyme from Archaeoglobus fulgidus, and its complexes with CTP and ATP at 2.0, 2.0 and 2.7 A resolutions, respectively. The geometry of the catalytic carboxylates and the relative positions of CTP and ATP to a single catalytic site are well conserved in both classes of CCA-adding enzymes, whereas the overall architectures, except for the catalytic core, of the class I and class II CCA-adding enzymes are fundamentally different. Furthermore, the recognition mechanisms of substrate nucleotides and tRNA molecules are distinct between these two classes, suggesting that the catalytic domains of class I and class II enzymes share a common origin, and distinct substrate recognition domains have been appended to form the two presently divergent classes."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg563"xsd:string
http://purl.uniprot.org/citations/14592988http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg563"xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Arisaka F."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Arisaka F."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Yokoyama S."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Yokoyama S."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Tomita K."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Tomita K."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Ishitani R."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Ishitani R."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Nureki O."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Nureki O."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Ishii R."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Ishii R."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Takeuchi N."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Takeuchi N."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Okabe M."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/author"Okabe M."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/14592988http://purl.uniprot.org/core/name"EMBO J."xsd:string