http://purl.uniprot.org/citations/29051530 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/29051530 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/29051530 | http://www.w3.org/2000/01/rdf-schema#comment | "Peptide macrocycles are promising therapeutic molecules because they are protease resistant, structurally rigid, membrane permeable, and capable of modulating protein-protein interactions. Here, we report the characterization of the dual function macrocyclase-peptidase enzyme involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles. The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate. Conformational trapping of the 25 amino-acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization. The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues. Structures of the enzyme bound to both substrates and biophysical analysis characterize the different binding modes rationalizing the mechanism. Using these insights simpler substrates with only five C-terminal residues were designed, allowing the enzyme to be more effectively exploited in biotechnology."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-017-00862-4"xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-017-00862-4"xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/author | "McMahon S.A."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/author | "McMahon S.A."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/author | "Naismith J.H."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/author | "Naismith J.H."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/author | "Czekster C.M."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/author | "Czekster C.M."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/author | "Ludewig H."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/author | "Ludewig H."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/name | "Nat. Commun."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/name | "Nat. Commun."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/pages | "1045"xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/pages | "1045"xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/title | "Characterization of a dual function macrocyclase enables design and use of efficient macrocyclization substrates."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/title | "Characterization of a dual function macrocyclase enables design and use of efficient macrocyclization substrates."xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/volume | "8"xsd:string |
http://purl.uniprot.org/citations/29051530 | http://purl.uniprot.org/core/volume | "8"xsd:string |
http://purl.uniprot.org/citations/29051530 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/29051530 |
http://purl.uniprot.org/citations/29051530 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/29051530 |