EC Number   |
|---|
    6.3.2.2 | 22.6 mg/ml purified enzyme, wild-type or mutant, hanging drop vapour diffusion method, equal volume of protein and reservoir solution, reservoir solution: 3.9 M sodium formate, pH 7.4, equilibration with reservoir solution at 293K, X-ray diffraction structure determination and analysis at 2.8 A resolution |
| 6.3.2.2 | hanging drop vapor diffusion method, crystal structure at 2.1 A resolution |
| 6.3.2.2 | homology model of the catalytic subunit of human glutamate cysteine ligase. Examination of the model suggests that post-translational modifications of cysteine residues may be involved in the regulation of enzymatic activity |
| 6.3.2.2 | sitting-drop vapor diffusion method, crystal structure of unliganded enzyme and enzyme complexed with a sulfoximine-based transition-state analog inhibitor at resolutions of 2.5 and 2.1 A, respectively. In the crystal structure of the complex, the bound inhibitor is phosphorylated at the sulfoximido nitrogen and is coordinated to three Mg2+ ions |
| 6.3.2.2 | structure of the GCL-glutathione complex to 2.5 A resolution indicates that the inhibitor occupies both the glutamate- and the presumed cysteine-binding site and disrupts the previously observed Mg2+-coordination in the ATP-binding site. The structure of the complex with mechanism-based inhibitor L-buthionine-S-sulfoximine to 2.2 A resolution confirms that L-buthionine-S-sulfoximine is phosphorylated on the sulfoximine nitrogen to generate the inhibitory species and reveals contacts that likely contribute to transition state stabilization |
| 6.3.2.2 | structures of glutamate cysteine ligase in the presence of glutamate and MgCl2, to 2.1 A resolution, and in complex with glutamate, MgCl2, and ADP to 2.7 A resolution. Structures reveal an unusual binding pocket for the alpha-carboxylate of the glutamate substrate and an ATP-independent Mg2+ coordination site, clarifying the Mg2+-dependence of the enzymatic reaction |
