EC Number   |
|---|
    2.7.7.27 | - |
| 2.7.7.27 | comparison of three-dimensional structure, substrate, and inhibitor binding specificity of AGPase small subunit from Oryza sativa ssp. japonica, Hordeum vulgare, and Triticum aestivum. Rearrangements of secondary structure elements, substrate, and inhibitor binding residues are strongly conserved and follow common folding pattern and orientation within monocot and dicot crop plants displaying a similar mode of allosteric regulation and catalytic mechanism |
| 2.7.7.27 | crystals of alpha-subunit are grown in high concentrations of sulfate, resulting in the sulfate-bound, allosterically inhibited form of the enzyme. Structures of the enzyme in complex with ATP and ADP-glucose |
| 2.7.7.27 | homology model of enzyme strucutre complexed with ADP-glucose |
| 2.7.7.27 | homology modeling of enzyme. In a heterodimeric structure, fifteen amino acids of the small subunit are able to make hydrophobic contacts with seventeen amino acids of the large subunit. A decrease in the solvent accessible surface area in the amino acids involved in interaction is also reported. Residues involved in hydrogen bonding are Thr422, Arg420, Ser259, Glu241, Gln113, and Gln70 of the small subunit to Met138, Gly47, Ser306, Ile311, Glu286 and Lys291 of the large subunit, respectively |
| 2.7.7.27 | isothermal titration calorimetry of substrate binding properties. The wild type heterotetramer possesses two distinct types of ATP binding sites, whereas the homotetrameric large/small subunit and small/small subunit variant forms only exhibit properties of one of the two binding sites. The wild type enzyme also exhibits significantly increased affinity to ATP compared to the homotetrameric enzyme forms. No stable binding is evident for glucose-1-phosphate, in the presence or absence of ATPgammaS supporting the Theorell-Chance bi-bi reaction mechanism |
| 2.7.7.27 | molecular modeling of enzyme. Binding of ATP correlates with conformational changes of a loop facing the ATP substrate, going from an open to a closed substrate-bound form |
| 2.7.7.27 | purified recombinant selenomethionyl-labeled enzyme anomalous selenomethionyl derivative, sitting drop vapor diffusion method, lithium sulfate as a precipitant, samples containing 5 mg/ml protein are mixed with an equal volume of 1.5 M lithium sulfate and 100 mM HEPES, pH 7.5, as the mother liquor, 1 week, mother liquor containing 20% v/v glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 2.1 A resolution, modelling with ATP and alpha-D-glucose-1-phosphate bound to the active site, overview |
| 2.7.7.27 | sitting-drop vapor-diffusion method using lithium sulfate as a precipitant, 2.0 A resolution, space group I222, crystals with unit-cell parameters a = 92.03, b = 141.251, c = 423.65 A |
