6eew | pdb_00006eew

Crystal structure of Catharanthus roseus tryptophan decarboxylase in complex with L-tryptophan

spinqualitylabelsall models 6eew, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6eew is a 4 chain structure with sequence from Catharanthus roseus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.0500207Å Ligands: CA, LLP, TRP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TDC_CATRO Catalyzes the decarboxylation of L-tryptophan to tryptamine and L-5-hydroxytryptophan to serotonin, respectively. Publication Abstract from PubMed Radiation of the plant pyridoxal 5'-phosphate (PLP)-dependent aromatic l-amino acid decarboxylase (AAAD) family has yielded an array of paralogous enzymes exhibiting divergent substrate preferences and catalytic mechanisms. Plant AAADs catalyze either the decarboxylation or decarboxylation-dependent oxidative deamination of aromatic l-amino acids to produce aromatic monoamines or aromatic acetaldehydes, respectively. These compounds serve as key precursors for the biosynthesis of several important classes of plant natural products, including indole alkaloids, benzylisoquinoline alkaloids, hydroxycinnamic acid amides, phenylacetaldehyde-derived floral volatiles, and tyrosol derivatives. Here, we present the crystal structures of four functionally distinct plant AAAD paralogs. Through structural and functional analyses, we identify variable structural features of the substrate-binding pocket that underlie the divergent evolution of substrate selectivity toward indole, phenyl, or hydroxyphenyl amino acids in plant AAADs. Moreover, we describe two mechanistic classes of independently arising mutations in AAAD paralogs leading to the convergent evolution of the derived aldehyde synthase activity. Applying knowledge learned from this study, we successfully engineered a shortened benzylisoquinoline alkaloid pathway to produce (S)-norcoclaurine in yeast. This work highlights the pliability of the AAAD fold that allows change of substrate selectivity and access to alternative catalytic mechanisms with only a few mutations. Structural basis for divergent and convergent evolution of catalytic machineries in plant aromatic amino acid decarboxylase proteins.,Torrens-Spence MP, Chiang YC, Smith T, Vicent MA, Wang Y, Weng JK Proc Natl Acad Sci U S A. 2020 May 5. pii: 1920097117. doi:, 10.1073/pnas.1920097117. PMID:32371491 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also DOPA decarboxylase

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