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http://purl.uniprot.org/citations/15351654http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15351654http://www.w3.org/2000/01/rdf-schema#comment"CheY is a member of the response regulator protein superfamily that controls the chemotactic swimming response of motile bacteria. The CheY double mutant D13K Y106W (CheY**) is resistant to phosphorylation, yet is a highly effective mimic of phosphorylated CheY in vivo and in vitro. The conformational attributes of this protein that enable it to signal in a phosphorylation-independent manner are unknown. We have solved the crystal structure of selenomethionine-substituted CheY** in the presence of its target, a peptide (FliM16) derived from the flagellar motor switch, FliM, to 1.5A resolution with an R-factor of 19.6%. The asymmetric unit contains four CheY** molecules, two with FliM16 bound, and two without. The two CheY** molecules in the asymmetric unit that are bound to FliM16 adopt a conformation similar to BeF3--activated wild-type CheY, and also bind FliM16 in a nearly identical manner. The CheY** molecules that do not bind FliM16 are found in a conformation similar to unphosphorylated wild-type CheY, suggesting that the active phenotype of this mutant is enabled by a facile interconversion between the active and inactive conformations. Finally, we propose a ligand-binding model for CheY and CheY**, in which Ile95 changes conformation in a Tyr/Trp106-dependent manner to accommodate FliM."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2004.07.084"xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/author"Dahlquist F.W."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/author"Lu J."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/author"Matthews B.W."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/author"McEvoy M.M."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/author"Campos A."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/author"Matsumura P."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/author"Hausrath A.C."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/author"Westbrook E.M."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/author"Quillin M.L."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/author"Dyer C.M."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/name"J Mol Biol"xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/pages"1325-1335"xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/title"Structure of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide."xsd:string
http://purl.uniprot.org/citations/15351654http://purl.uniprot.org/core/volume"342"xsd:string
http://purl.uniprot.org/citations/15351654http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15351654
http://purl.uniprot.org/citations/15351654http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15351654
http://purl.uniprot.org/uniprot/#_P0AE67-mappedCitation-15351654http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15351654
http://purl.uniprot.org/uniprot/#_P06974-mappedCitation-15351654http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15351654
http://purl.uniprot.org/uniprot/P06974http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15351654
http://purl.uniprot.org/uniprot/P0AE67http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15351654