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http://purl.uniprot.org/citations/10622255http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10622255http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10622255http://www.w3.org/2000/01/rdf-schema#comment"Receiver domains are the dominant molecular switches in bacterial signalling. Although several structures of non-phosphorylated receiver domains have been reported, a detailed structural understanding of the activation arising from phosphorylation has been impeded by the very short half-lives of the aspartylphosphate linkages. Here we present the first structure of a receiver domain in its active state, the phosphorylated receiver domain of the bacterial enhancer-binding protein NtrC (nitrogen regulatory protein C). Nuclear magnetic resonance spectra were taken during steady-state autophosphorylation/dephosphorylation, and three-dimensional spectra from multiple samples were combined. Phosphorylation induces a large conformational change involving a displacement of beta-strands 4 and 5 and alpha-helices 3 and 4 away from the active site, a register shift and an axial rotation in helix 4. This creates an exposed hydrophobic surface that is likely to transmit the signal to the transcriptional activation domain."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.org/dc/terms/identifier"doi:10.1038/47273"xsd:string
http://purl.uniprot.org/citations/10622255http://purl.org/dc/terms/identifier"doi:10.1038/47273"xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Kern D."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Kern D."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Wemmer D.E."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Wemmer D.E."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Volkman B.F."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Volkman B.F."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Luginbuhl P."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Luginbuhl P."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Kustu S."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Kustu S."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Nohaile M.J."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/author"Nohaile M.J."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/pages"894-898"xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/pages"894-898"xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/title"Structure of a transiently phosphorylated switch in bacterial signal transduction."xsd:string
http://purl.uniprot.org/citations/10622255http://purl.uniprot.org/core/title"Structure of a transiently phosphorylated switch in bacterial signal transduction."xsd:string