Structural Studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1Q1L, 1QXO, 1R52, 1R53, 1SQ1, 1UM0, 1UMF, 1ZTB, and 2G85.
The crystal structure of chorismate sythase is a homotetramer with one FMN molecule non-covalently bound to each of the four monomers. Each monomer is made up of 9 alpha helices and 18 beta strands and the core is assembled in a unique beta-alpha-beta sandwich fold. The active sites for FMN-binding are made up of clusters of flexible loops and the area around these regions have highly positive electromagnetic potential. There are two histidine residues located at the active site which are thought to protonate the reduced flavin molecule and the leaving phosphate group of the substrate.
Read more about this topic: Chorismate Synthase
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