EC Number   |
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    2.4.2.28 | analysis of the crystal packing. Space group is C2, unit-cell parameters are a = 135.16, b = 138.09, c = 96.56 A, beta = 92.21°. The asymmetric unit contains two independent half-hexamers, the other half of each of which is generated by a crystallographic twofold axis |
| 2.4.2.28 | apoenzyme and in complex with rhodamine B, hanging drop vapor diffusion method, using 35% (w/v) PPG 400, 75 mM MgCl2 and 0.1 M Bis-Tris pH 6.5 |
| 2.4.2.28 | crystal structures of apo MTAP and MTAP in complex with p-Cl-PhT-DADMe-ImmA are determined at 1.9 and 2.0 A resolution, respectively. Inhibitor binding causes condensation of the enzyme active site, reorganization at the trimer interfaces, the release of water from the active sites and subunit interfaces, and compaction of the trimeric structure. These structural changes cause the entropy-favored binding of transition state analogues |
| 2.4.2.28 | crystals are grown at either room temperature or 18°C using the hanging drop vapor diffusion technique. Determination of the structure of 5'-deoxy-5'-methylthioadenosine phosphorylase alone, as ternary complexes with sulfate plus substrates 5'-deoxy-5'-methylthioadenosine, adenosine, or guanosine, or with the noncleavable substrate analog formycin B and as binary complexes with phosphate or sulfate alone. The structure of unliganded SsMTAP is refined at 2.5 A resolution and the structures of the complexes are refined at resolutions ranging from 1.6 A to 2.0 A |
| 2.4.2.28 | from recombinant enzyme, hanging drop-vapour diffusion method, protein 25 mg/ml, 10 mM Tris-HCl, pH 7.4, 5 mM DTT, 0.4 M NaCl against reservoir solution of 80 mM MES, pH 5.9, 5 mM DTT, 12% w/v polyethylene glycol 6000, 25% v/v ethylene glycol, in presence of substrates adenine, phosphate and sulfate, structure analysis by X-ray diffraction at light scattering |
| 2.4.2.28 | from recombinant enzyme, hanging drop-vapour diffusion method, protein solution, 7-10 mg/ml, 18°C, reservoir solution for native crystals: Tris-HCl 10 mM, pH 7.4, 28-30% dioxane, 12% 2-methyl-2,4-pentanediol, 0.12 M MgCl2, 0,04 M NaCl, for crystals of enzyme complexed with substrates or sulfate and phosphate ions, substrates are added and NaCl is exchanged for MgSO4 or NH4Cl and KH2PO4, respectively, X-ray structure determination and analysis |
| 2.4.2.28 | hanging-drop, vapor-diffusion method at 22°C, the crystal structure of the enzyme in complex with 5'-deoxy-5'-methylthioadenosine and sulfate is determined to 1.45 A resolution |
| 2.4.2.28 | in complex with 5'-methylthio-DADMe-immucillin A, 5'-butylthio-DADMe-immucillin A, 5'-propylthio-immucillin A or 5'-methylthio-tubercidin, sitting drop vapor diffusion method, using 0.2 M magnesium chloride, 0.1 M sodium citrate:citric acid (pH 5.5), and 40% (w/v) PEG 400 for 5'-methylthio-DADMe-immucillin A or 5'-propylthio-immucillin A, 3 M sodium chloride and 0.1 M sodium acetate (pH 4.5) for BT-DADMe-immucillin A, and 0.2 M magnesium chloride and 20% (w/v) PEG 3350 for 5'-methylthio-tubercidin |
| 2.4.2.28 | in complex with adenine, 5'-deoxy-5'-methylthioadenosine, tubercidin or sulfate, hanging drop vapor diffusion method, using 100 mM Bis-Tris or MES buffer, pH 6.1-6.7 and 14-18% (w/v) PEG 3350 |
| 2.4.2.28 | in complex with adenine, by sitting- and hanging-drop formation at 22°C, at 2.9 A resolution. Belongs to space group P3121, monomer consists of seven alpha-helices, ten beta-strands, and a 3(10)-helix. Residues between 216 and 225 demonstrate weak electron density for both subunits, therefore indicating this loop has high flexibility. Bound adenine is located in the deep pocket formed by the monomer with the entrance partially covered by the adjacent subunit. This flap is critical in the formation of a wide dimer interface |
