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http://purl.uniprot.org/citations/8502994http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8502994http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8502994http://www.w3.org/2000/01/rdf-schema#comment"Pectate lyases are secreted by pathogens and initiate soft-rot diseases in plants by cleaving polygalacturonate, a major component of the plant cell wall. The three-dimensional structure of pectate lyase C from Erwinia chrysanthemi has been solved and refined to a resolution of 2.2 angstroms. The enzyme folds into a unique motif of parallel beta strands coiled into a large helix. Within the core, the amino acids form linear stacks and include a novel asparagine ladder. The sequence similarities that pectate lyases share with pectin lyases, pollen and style proteins, and tubulins suggest that the parallel beta helix motif may occur in a broad spectrum of proteins."xsd:string
http://purl.uniprot.org/citations/8502994http://purl.org/dc/terms/identifier"doi:10.1126/science.8502994"xsd:string
http://purl.uniprot.org/citations/8502994http://purl.org/dc/terms/identifier"doi:10.1126/science.8502994"xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/author"Keen N.T."xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/author"Keen N.T."xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/author"Jurnak F."xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/author"Jurnak F."xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/author"Yoder M.D."xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/author"Yoder M.D."xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/pages"1503-1507"xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/pages"1503-1507"xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/title"New domain motif: the structure of pectate lyase C, a secreted plant virulence factor."xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/title"New domain motif: the structure of pectate lyase C, a secreted plant virulence factor."xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/volume"260"xsd:string
http://purl.uniprot.org/citations/8502994http://purl.uniprot.org/core/volume"260"xsd:string
http://purl.uniprot.org/citations/8502994http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8502994
http://purl.uniprot.org/citations/8502994http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8502994
http://purl.uniprot.org/citations/8502994http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8502994
http://purl.uniprot.org/citations/8502994http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8502994