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http://purl.uniprot.org/citations/21168411http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21168411http://www.w3.org/2000/01/rdf-schema#comment"Room temperature neutron diffraction data of the fully perdeuterated Toho-1 R274N/R276N double mutant β-lactamase in the apo form were used to visualize deuterium atoms within the active site of the enzyme. This perdeuterated neutron structure of the Toho-1 R274N/R276N reveals the clearest picture yet of the ground-state active site protonation states and the complete hydrogen-bonding network in a β-lactamase enzyme. The ground-state active site protonation states detailed in this neutron diffraction study are consistent with previous high-resolution X-ray studies that support the role of Glu166 as the general base during the acylation reaction in the class A β-lactamase reaction pathway."xsd:string
http://purl.uniprot.org/citations/21168411http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2010.12.017"xsd:string
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/author"Cooper J."xsd:string
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/author"Coates L."xsd:string
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/author"Weiss K.L."xsd:string
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/author"Wang K.K."xsd:string
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/author"Blakeley M.P."xsd:string
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/author"Tomanicek S.J."xsd:string
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/pages"364-368"xsd:string
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/title"The active site protonation states of perdeuterated Toho-1 beta-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation."xsd:string
http://purl.uniprot.org/citations/21168411http://purl.uniprot.org/core/volume"585"xsd:string
http://purl.uniprot.org/citations/21168411http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21168411
http://purl.uniprot.org/citations/21168411http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21168411
http://purl.uniprot.org/uniprot/#_Q47066-mappedCitation-21168411http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21168411
http://purl.uniprot.org/uniprot/Q47066http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21168411