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http://purl.uniprot.org/citations/26627834http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26627834http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26627834http://www.w3.org/2000/01/rdf-schema#comment"Carnivorous plants primarily use aspartic proteases during digestion of captured prey. In contrast, the major endopeptidases in the digestive fluid of the Venus flytrap (Dionaea muscipula) are cysteine proteases (dionain-1 to -4). Here, we present the crystal structure of mature dionain-1 in covalent complex with inhibitor E-64 at 1.5 Å resolution. The enzyme exhibits an overall protein fold reminiscent of other plant cysteine proteases. The inactive glycosylated pro-form undergoes autoprocessing and self-activation, optimally at the physiologically relevant pH value of 3.6, at which the protective effect of the pro-domain is lost. The mature enzyme was able to efficiently degrade a Drosophila fly protein extract at pH 4 showing high activity against the abundant Lys- and Arg-rich protein, myosin. The substrate specificity of dionain-1 was largely similar to that of papain with a preference for hydrophobic and aliphatic residues in subsite S2 and for positively charged residues in S1. A tentative structure of the pro-domain was obtained by homology modeling and suggested that a pro-peptide Lys residue intrudes into the S2 pocket, which is more spacious than in papain. This study provides the first analysis of a cysteine protease from the digestive fluid of a carnivorous plant and confirms the close relationship between carnivorous action and plant defense mechanisms."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.org/dc/terms/identifier"doi:10.1074/JBC.M115.672550"xsd:string
http://purl.uniprot.org/citations/26627834http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m115.672550"xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Garcia-Ferrer I."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Garcia-Ferrer I."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Gomis-Ruth F.X."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Gomis-Ruth F.X."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Enghild J.J."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Enghild J.J."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Guevara T."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Guevara T."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Thogersen I.B."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Thogersen I.B."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Rossen L."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Rossen L."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Sanggaard K.W."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Sanggaard K.W."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Scavenius C."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Scavenius C."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Lukassen M.V."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Lukassen M.V."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Thomsen L.R."xsd:string
http://purl.uniprot.org/citations/26627834http://purl.uniprot.org/core/author"Thomsen L.R."xsd:string