EC Number   |
|---|
    4.2.3.5 | - |
| 4.2.3.5 | beta-alpha-beta sandwich structure |
| 4.2.3.5 | crystal structure of chorismate synthase in both FMN-bound and FMN-free form. It is a tetrameric enzyme, with each monomer possessing a novel beta-alpha-beta sandwich fold |
| 4.2.3.5 | crystal structure of the enzyme reveals a novel beta alpha beta sandwich topology |
| 4.2.3.5 | hanging drop vapour diffusion method, three-dimensional X-ray structure from selenomethionine-labeled crystals at 2.2 A resolution. The structure shows a novel beta,alpha,beta,alpha fold consisting of an alternate tight packing of two alpha-helical and two beta-sheet layers. The molecule is arranged as a tight tetramer with D2 symmetry |
| 4.2.3.5 | hanging-drop vapour diffusion method. Crystal streucture solved at 1.0 A |
| 4.2.3.5 | hanging-drop vapour-diffusion method, crystallization at 296 K using polyethylene glycol 400 as precipitant, recombinant enzyme fused with an eight-residue C-terminal tag |
| 4.2.3.5 | homology modeling of structure of chorismate synthase along with cofactor FMN using crystal structure of Helicobacter pylori chorismate synthase. Each monomer of Plasmodium falciparum chorismate synthase consists of 10 helices and 13 sheets. The core of monomer has a unique beta-alpha-beta sandwich fold that appears as a three layered structure in the predicted model. This unique fold consists of two antiparallel five stranded beta-sheet layers and four alpha-helices which are sandwiched between these two beta-sheet layers. The unique beta-alpha-beta-sandwich provides a scaffold for cofactor and substrate binding. The residues involved in polar interactions with substrate 5-enolpyruvylshikimate-3-phosphate are Arg46, Lys60, Asp61, Lys90, Ser121, Ser122 and Arg491 |
| 4.2.3.5 | modelling the conversion of 5-enolpyruvylshikimate-3-phosphate to chorismate in chorismate synthase unsing B3LYP density functional theory and ab initio QM/MM methods, based on PDB entry 1QXO. In the reaction mechanism phosphate elimination precedes proton transfer. B3LYP predicts reaction energetics that are qualitatively wrong |
