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http://purl.uniprot.org/citations/8421502http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8421502http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8421502http://www.w3.org/2000/01/rdf-schema#comment"The histidine-containing phosphocarrier protein (HPr) is a central component of the phosphoenolpyruvate: sugar phosphotransferase system that transports carbohydrates across the cell membrane of bacteria. A typical phosphotransfer sequence is phosphoenolpyruvate-->enzyme I-->HPr-->enzyme II/IIIsugar-->sugar. This is thermodynamically favourable owing to the participation of the high-energy phosphoenolpyruvate. We report here the structure of HPr from Streptococcus faecalis determined at 1.6 A resolution. Remarkable disallowed Ramachandran torsion angles at the active centre, revealed by the X-ray structure, demonstrate a unique example of torsion-angle strain that is probably directly involved in protein function. During phosphorylation, the active-centre torsion-angle strain should facilitate the phosphotransfer reaction by lowering the activation-energy barrier. A recently reported Bacillus subtilis HPr structure, which represents the phosphorylated state of HPr with no torsion-angle strain, provides direct evidence supporting our hypothesis that torsion-angle strain plays a direct part in the function of HPr. An HPr phosphotransfer cycling mechanism is proposed, based primarily on the structures of HPr and other phosphotransferase system proteins."xsd:string
http://purl.uniprot.org/citations/8421502http://purl.org/dc/terms/identifier"doi:10.1038/361094a0"xsd:string
http://purl.uniprot.org/citations/8421502http://purl.org/dc/terms/identifier"doi:10.1038/361094a0"xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/author"Jia Z."xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/author"Jia Z."xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/author"Quail J.W."xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/author"Quail J.W."xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/author"Vandonselaar M."xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/author"Vandonselaar M."xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/author"Delbaere L.T.J."xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/author"Delbaere L.T.J."xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/pages"94-97"xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/pages"94-97"xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/title"Active-centre torsion-angle strain revealed in 1.6 A-resolution structure of histidine-containing phosphocarrier protein."xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/title"Active-centre torsion-angle strain revealed in 1.6 A-resolution structure of histidine-containing phosphocarrier protein."xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/volume"361"xsd:string
http://purl.uniprot.org/citations/8421502http://purl.uniprot.org/core/volume"361"xsd:string
http://purl.uniprot.org/citations/8421502http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8421502
http://purl.uniprot.org/citations/8421502http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8421502