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http://purl.uniprot.org/citations/28712808http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28712808http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28712808http://www.w3.org/2000/01/rdf-schema#comment"Protein kinases play central roles in the survival of Mycobacterium tuberculosis within host. Here we report the individual high-resolution crystal structures of the sensor domain (in both monomer and dimer forms) and the kinase domain of PknI, a transmembrane protein member of the serine/threonine protein kinases (STPKs) family. PknI is the first STPK identified whose sensor domain exists in a monomer-dimer equilibrium. Inspection of the two structures of the sensor domain (PknI_SD) revealed conformational changes upon dimerization, with an arm region of critical importance for dimer formation identified. Rapamycin-induced dimerization of unphosphorylated fusions of PknI juxtamembrane and the kinase domain, intended to mimic the dimerization effect presumably imposed by PknI_SD, was observed to be able to activate auto-phosphorylation activity of the kinase domain. In vivo experiments using an M. bovis model suggested PknI functions as a dimer in the regulation of M. tuberculosis growth."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2017.06.010"xsd:string
http://purl.uniprot.org/citations/28712808http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2017.06.010"xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Rao Z."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Rao Z."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Zhang Q."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Zhang Q."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Zhang W."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Zhang W."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Yang H."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Yang H."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Yan Q."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Yan Q."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Zhou W."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Zhou W."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Jiang D."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Jiang D."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Qian L."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Qian L."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Mi K."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Mi K."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Guddat L."xsd:string
http://purl.uniprot.org/citations/28712808http://purl.uniprot.org/core/author"Guddat L."xsd:string