Results

RDF/XMLNTriplesTurtleShow queryShare ▶
SubjectPredicateObject
http://purl.uniprot.org/citations/7500360http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7500360http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7500360http://www.w3.org/2000/01/rdf-schema#comment"Kinetic and crystallographic studies have characterized the effect of 2-deoxy-glucose 6-phosphate on the catalytic and structural properties of glycogen phosphorylase b. Previous work on the binding of glucose 6-phosphate, a potent physiological inhibitor of the enzyme, to T state phosphorylase b in the crystal showed that the inhibitor binds at the allosteric site and induces substantial conformational changes that affect the subunit-subunit interface. The hydrogen-bond from the O-2 hydroxyl of glucose 6-phosphate to the main-chain oxygen of Val40' represents the only hydrogen bond from the sugar to the other subunit, and this interaction appears important for promoting a more "tensed" structure than native T state phosphorylase b. 2-Deoxy-glucose 6-phosphate acts competitively with both the activator AMP and the substrate glucose 1-phosphate, with Ki values of 0.53 mM and 1.23 mM, respectively. The binding of 2-deoxy-glucose 6-phosphate to T state glycogen phosphorylase b in the crystal, has been investigated and the complex phosphorylase b: 2-deoxy-glucose 6-phosphate has been refined to give a crystallographic R factor of 17.3%, for data between 8 A and 2.3 A. 2-Deoxy-glucose 6-phosphate binds at the allosteric site as the a anomer and adopts a different conformation compared to glucose 6-phosphate. The two conformations differ by 160 degrees in the torsion angle about the C-5-C-6 bond. The contacts from the phosphate group are essentially identical to those made by the phosphate of glucose 6-phosphate but the 2-deoxy glucosyl moiety binds in a quite different orientation compared to the glucosyl of glucose 6-phosphate. 2-Deoxy-glucose 6-phosphate can be accommodated in the allosteric site with very little change in the protein, while structural comparisons show that the phosphorylase b: 2-deoxy-glucose 6-phosphate complex structure is overall more similar to a glucose-like complex than to the Glc-6-P complex structure."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1995.0665"xsd:string
http://purl.uniprot.org/citations/7500360http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1995.0665"xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/author"Acharya K.R."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/author"Acharya K.R."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/author"Papageorgiou A.C."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/author"Papageorgiou A.C."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/author"Johnson L.N."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/author"Johnson L.N."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/author"Zographos S.E."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/author"Zographos S.E."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/author"Oikonomakos N.G."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/author"Oikonomakos N.G."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/pages"900-917"xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/pages"900-917"xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/title"The binding of 2-deoxy-D-glucose 6-phosphate to glycogen phosphorylase b: kinetic and crystallographic studies."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/title"The binding of 2-deoxy-D-glucose 6-phosphate to glycogen phosphorylase b: kinetic and crystallographic studies."xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/volume"254"xsd:string
http://purl.uniprot.org/citations/7500360http://purl.uniprot.org/core/volume"254"xsd:string
▶