EC Number   |
|---|
    6.3.1.2 | - |
| 6.3.1.2 | apo-enzyme structure determination and analysis at resolution of 3.0 A, molecular replacement using a pentamer of Zea mays GS/MnADP/MSO-P complex, overview |
| 6.3.1.2 | complex of the enzyme with the purine analogue 1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-dione alone to 2.55 A resolution, and in complex with 1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-dione together with methionine sulfoximine phosphate, magnesium and phosphate, to 2.2 A resolution. The former represents a relaxed, inactive conformation of the enzyme, while the latter is a taut, active one. Compound 1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-dione binds at the same position in the nucleotide site, regardless of the conformational state |
| 6.3.1.2 | computational study on folding state |
| 6.3.1.2 | enzyme complexed with 3, X-ray diffraction structure determination and analysis |
| 6.3.1.2 | four crystal structures of glutamine synthetase, complexed with the substrate Glu and with each of the three feddback inhibitors, Gly, Ala, and Ser |
| 6.3.1.2 | hanging drop vapour diffusion method, GS crystals in complex with ADP and methionine sulfoximine phosphate, using 9% (w/v) polyethylene glycol 8000, 100 mM Tris-HCl pH 7.8, 5% (v/v) 2-methyl-2,4-pentanediol, 10 mM MnCl2 |
| 6.3.1.2 | purified recombinant detagged apo-enzyme, enzyme-glutamate-AMPPCP complex, and enzyme transition state, hanging drop vapor diffusion, for enzyme-glutamate-AMPPCP crystals: mixing of 40 mg/ml protein at a 1:1 ratio with 40% 4-methyl-2,4-pentanediol and 200 mM MgSO4, and inverting the drop over the reservoir solution containing 15% PEG 8000, 0.1 M HEPES, pH 7.5, and 10 mM MgCl2, for enzyme-L-methionine-S-sulfoximine-phosphate-ADP crystals: mixing of 40 mg/ml protein with 5 mM MgCl2, 5 mM ATP, and 5 mM L-methionine-S-sulfoximine,and combining in a 1:1 ratio with crystallization reagent containing 10% PEG 4000, 0.1 M HEPES, pH 7.5, for apo-enzyme crystals: mixing the protein 40 mg/ml at a 1:1 ratio with 40% 4-methyl-2,4-pentanediol and 200 mM MgSO4 and inverting the drop over the reservoir solution, room temperature, X-ray diffraction structure determination and analysis at 3.1 A, 2.87 A, and 2.58 A resolution, respectively |
| 6.3.1.2 | structural model for the reaction mechanism of glutamine synthetase, based on five crystal structures of enzyme-substrate complexes |
| 6.3.1.2 | Ta6Br12 derivative, to 3.5 A resolution, space group C2221. The divergence of the type III from the type I and II GS enzymes is mainly due to differences in quaternary structure despite all the enzymes sharing a remarkably conserved active site fold.. The two hexameric rings of the GSIII dodecamer associate on the opposite surface relative to types I and II |
