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http://purl.uniprot.org/citations/27273476http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27273476http://www.w3.org/2000/01/rdf-schema#comment"A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. The mechanism of chaperone-mediated P-ring formation is poorly understood. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain. Pull-down experiments support a specific protein-protein interaction between FlgI, the P-ring component protein, and the C-terminal domain of FlgA. Surface plasmon resonance and limited-proteolysis indicate that flexibility of the domain is reduced in the covalently closed form. These results show that the structural flexibility of the C-terminal domain of FlgA, which is related to the structural difference between the two crystal forms, is intrinsically associated with its molecular chaperone function in P-ring assembly."xsd:string
http://purl.uniprot.org/citations/27273476http://purl.org/dc/terms/identifier"doi:10.1038/srep27399"xsd:string
http://purl.uniprot.org/citations/27273476http://purl.uniprot.org/core/author"Namba K."xsd:string
http://purl.uniprot.org/citations/27273476http://purl.uniprot.org/core/author"Matsunami H."xsd:string
http://purl.uniprot.org/citations/27273476http://purl.uniprot.org/core/author"Samatey F.A."xsd:string
http://purl.uniprot.org/citations/27273476http://purl.uniprot.org/core/author"Meshcheryakov V.A."xsd:string
http://purl.uniprot.org/citations/27273476http://purl.uniprot.org/core/author"Yoon Y.H."xsd:string
http://purl.uniprot.org/citations/27273476http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27273476http://purl.uniprot.org/core/name"Sci Rep"xsd:string
http://purl.uniprot.org/citations/27273476http://purl.uniprot.org/core/pages"27399"xsd:string
http://purl.uniprot.org/citations/27273476http://purl.uniprot.org/core/title"Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica."xsd:string
http://purl.uniprot.org/citations/27273476http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/27273476http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27273476
http://purl.uniprot.org/citations/27273476http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27273476
http://purl.uniprot.org/uniprot/#_P40131-mappedCitation-27273476http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27273476
http://purl.uniprot.org/uniprot/P40131http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27273476