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4.2.3.5: chorismate synthase

This is an abbreviated version!
For detailed information about chorismate synthase, go to the full flat file.

Word Map on EC 4.2.3.5

Reaction

5-O-(1-carboxyvinyl)-3-phosphoshikimate
=
chorismate
 +
phosphate

Synonyms

5-enolpyruvylshikimate-3-phosphate phospholyase, 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate lyase, ARO2, aroC, aroF, chorismate synthase, chorismate synthetase, CS, CS1, CS2, EC 4.6.1.4, MtCS, VEG216, Vegetative protein 216, Vlaro2

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.5 chorismate synthase

Crystallization

Crystallization on EC 4.2.3.5 - chorismate synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme reveals a novel beta alpha beta sandwich topology
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
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
-
beta-alpha-beta sandwich structure
-
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
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
hanging-drop vapour diffusion method. Crystal streucture solved at 1.0 A
-
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