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http://purl.uniprot.org/citations/9336834http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9336834http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9336834http://www.w3.org/2000/01/rdf-schema#comment"The histidine-containing protein (HPr) of bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) serves a central role in a series of phosphotransfer reactions used for the translocation of sugars across cell membranes. These studies report the high-definition solution structures of both the unphosphorylated and histidine phosphorylated (P-His) forms of HPr from Bacillus subtilis. Consistent with previous NMR studies, local conformational adjustments occur upon phosphorylation of His 15, which positions the phosphate group to serve as a hydrogen bond acceptor for the amide protons of Ala 16 and Arg 17 and to interact favorably with the alpha-helix macrodipole. However, the positively charged side chain of the highly conserved Arg 17 does not appear to interact directly with phospho-His 15, suggesting that Arg 17 plays a role in the recognition of other PTS enzymes or in phosphotransfer reactions directly. Unlike the results reported for Escherichia coli P-His HPr (Van Nuland NA, Boelens R, Scheek RM, Robillard GT, 1995, J Mol Biol 246:180-193), our data indicate that phosphorylation of His 15 is not accompanied by adoption of unfavorable backbone conformations for active site residues in B. subtilis P-Ser HPr."xsd:string
http://purl.uniprot.org/citations/9336834http://purl.org/dc/terms/identifier"doi:10.1002/pro.5560061006"xsd:string
http://purl.uniprot.org/citations/9336834http://purl.org/dc/terms/identifier"doi:10.1002/pro.5560061006"xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/author"Klevit R.E."xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/author"Klevit R.E."xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/author"Jones B.E."xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/author"Jones B.E."xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/author"Rajagopal P."xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/author"Rajagopal P."xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/pages"2107-2119"xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/pages"2107-2119"xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/title"Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis."xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/title"Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis."xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/9336834http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/9336834http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9336834
http://purl.uniprot.org/citations/9336834http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9336834
http://purl.uniprot.org/citations/9336834http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9336834
http://purl.uniprot.org/citations/9336834http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9336834