Fig. 1: Structure of L-tryptophan decarboxylase PsiD.
a Enzymatic synthesis pathway of psilocybin in P. cubensis. The reaction scheme was redrawn from a previous study24. b Schematic representation of the catabolic substrate and product of the PsiD protein. c The schematic depicts the self-cleavage mechanism of PsiD from the proenzyme to the mature enzyme. d The overall structure of the PsiD protein. The α-chain is colored cyan, and the β-chain is colored green. The pyruvoyl group is shown as sticks. e The potential reaction scheme for the self-cleavage of the PsiD proenzyme. f The distance between the C-terminal of the β-chain Gly402 and the N-terminal Pvl403 of the α-chain after self-cleavage. The residues G402 and Pvl403 are shown as sticks. The |Fo|-|Fc| map is contoured at 3.0 σ (colored blue). g The four loop regions responsible for pocket formation are colored yellow, blue, cyan, and purple, respectively. h The electrostatic surface representation of the substrate-binding pocket. The pocket region containing Pvl403 is indicated by a blue circle.
