Tryptophan synthase

spinqualitylabelsall models Tryptophan synthaseα subunit (yellow, salmon) and β subunit (cyan, green) of the α2β2 tetramer complex with pyridoxal-phosphate, glycerol-3-phosphate and Na+ ion (purple) 1wbj Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Tryptophan synthase (TrpS) is an α2β2 tetramer participating in the biosynthesis of tryptophan. TrpS α subunit catalyzes the formation of indole and glyceraldehyde-3-phosphate (G3P) from indole-3-glycerol phosphate (IGP). The β subunit catalyzes in a pyridoxal-phosphate (PLP) dependent reaction the formation of tryptophan (Trp) from indole and serine. The diffusion of indole from the α to the β subunit is facilitated via a hydrophobic channel connecting the subunits. Relevance TrpS is not found in animals hence it is tested as a possible drug target for tuberculosis, ocular and genital infections, cryptosporidiosis and as herbicide. Structural highlights The active site of TrpS subunit α contains the catalytic residues Glu and Asp. Water molecules are shown as red spheres. 3D structures of tryptophan synthase Tryptophan synthase 3D structures

References

↑Abrahams, K. A., Cox, J., Fütterer, K., Rullas, J., Ortega-Muro, F., Loman, N. J., Moynihan, P. J., Pérez-Herrán, E., Jiménez, E., Esquivias, J., Barros, D., Ballell, L., Alemparte, C., & Besra, G. S. (2017). Inhibiting mycobacterial tryptophan synthase by targeting the inter-subunit interface. Scientific reports, 7(1), 9430.

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