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http://purl.uniprot.org/citations/20606265http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20606265http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20606265http://www.w3.org/2000/01/rdf-schema#comment"Aspartates in proteins are isomerized non-enzymatically to isoaspartate via succinimide in vitro and in vivo. In order to elucidate the mechanism of isoaspartate formation within the Asp45-Glu46 sequence of Ustilago sphaerogena ribonuclease U2 based on three-dimensional structure, crystal structures of ribonuclease U2 complexed with adenosine 3'-monophosphate have been solved at 0.96 and 0.99 A resolution. The crystal structures revealed that the C(gamma) atom of Asp45 is located just beside the main-chain N atom of Glu46 and that the conformation which is suitable for succinimide formation is stabilized by a hydrogen-bond network mediated by water molecules 190, 219 and 220. These water molecules are suggested to promote the formation of isoaspartate via succinimide: in the succinimide-formation reaction water 219 receives a proton from the N atom of Glu46 as a general base and waters 190 and 220 stabilize the tetrahedral intermediate, and in the succinimide-hydrolysis reaction water 219 provides a proton for the N atom of Glu46 as a general acid. The purine-base recognition scheme of ribonuclease U2 is also discussed."xsd:string
http://purl.uniprot.org/citations/20606265http://purl.org/dc/terms/identifier"doi:10.1107/s0907444910019621"xsd:string
http://purl.uniprot.org/citations/20606265http://purl.org/dc/terms/identifier"doi:10.1107/s0907444910019621"xsd:string
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/author"Noguchi S."xsd:string
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/author"Noguchi S."xsd:string
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/pages"843-849"xsd:string
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/pages"843-849"xsd:string
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/title"Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-monophosphate."xsd:string
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/title"Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-monophosphate."xsd:string
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/volume"66"xsd:string
http://purl.uniprot.org/citations/20606265http://purl.uniprot.org/core/volume"66"xsd:string
http://purl.uniprot.org/citations/20606265http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20606265
http://purl.uniprot.org/citations/20606265http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20606265
http://purl.uniprot.org/citations/20606265http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20606265
http://purl.uniprot.org/citations/20606265http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20606265
http://purl.uniprot.org/uniprot/P00654http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/20606265
http://purl.uniprot.org/uniprot/#_P00654-citation-20606265http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20606265