RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/35278475http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35278475http://www.w3.org/2000/01/rdf-schema#comment"As one of the most valuable tools for genetic code expansion, pyrrolysyl-tRNA synthetase (PylRS) is structurally related to phenylalanyl-tRNA synthetase (PheRS). By introducing mutations that mimic ligand interactions in PheRS into PylRS, we designed a PylRS mutant. This mutant, designated as oClFRS, recognizes a number of o-substituted phenylalanines for their genetic incorporation at amber codon. Its efficiency in catalyzing genetic incorporation of o-chlorophenylalanine (o-ClF) is better than that for Nε-tert-butyloxycarbonyl-lysine catalyzed by PylRS. The crystal structure of oClFRS bound with o-ClF shows that o-ClF binds deeply into a hydrophobic but catalytically inactive pocket in the active site and involves two halogen bonds to achieve strong interactions. The shift of o-ClF to a catalytically active position in the oClFRS active site will be necessary for its activation. This is the first reported aminoacyl-tRNA synthetase that involves two halogen bonds for ligation recognition and might represent an alternative route to develop aminoacyl-tRNA synthetase mutants that are selective for noncanonical amino acids over native amino acids."xsd:string
http://purl.uniprot.org/citations/35278475http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2022.167534"xsd:string
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/author"Qiao Y."xsd:string
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/author"Xu S."xsd:string
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/author"Yang K.S."xsd:string
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/author"Liu W.R."xsd:string
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/author"Geng Z.Z."xsd:string
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/author"Vatansever E.C."xsd:string
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/name"J Mol Biol"xsd:string
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/pages"167534"xsd:string
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/title"A Designed, Highly Efficient Pyrrolysyl-tRNA Synthetase Mutant Binds o-Chlorophenylalanine Using Two Halogen Bonds."xsd:string
http://purl.uniprot.org/citations/35278475http://purl.uniprot.org/core/volume"434"xsd:string
http://purl.uniprot.org/citations/35278475http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/35278475
http://purl.uniprot.org/citations/35278475http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/35278475
http://purl.uniprot.org/uniprot/#_Q8PWY1-mappedCitation-35278475http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35278475
http://purl.uniprot.org/uniprot/Q8PWY1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/35278475