5hsj | pdb_00005hsj

Structure of tyrosine decarboxylase complex with PLP at 1.9 Angstroms resolution

spinqualitylabelsall models 5hsj, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5hsj is a 2 chain structure with sequence from Levilactobacillus brevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TYRDC_LEVBR Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:24211777, PubMed:27292129). Cannot use other aromatic L-amino acids as substrates like L-phenylalanine, L-tryptophan and L-glutamate (PubMed:24211777). Is also able to decarboxylate the Parkinson's disease medication levodopa (L-dopa) to dopamine in vitro. Publication Abstract from PubMed Tyrosine decarboxylase (TDC) is a pyridoxal 5-phosphate (PLP)-dependent enzyme and is mainly responsible for the synthesis of tyramine, an important biogenic amine. In this study, the crystal structures of the apo and holo forms of Lactobacillus brevis TDC (LbTDC) were determined. The LbTDC displays only 25% sequence identity with the only reported TDC structure. Site-directed mutagenesis of the conformationally flexible sites and catalytic center was performed to investigate the potential catalytic mechanism. It was found that H241 in the active site plays an important role in PLP binding because it has different conformations in the apo and holo structures of LbTDC. After binding to PLP, H241 rotated to the position adjacent to the PLP pyridine ring. Alanine scanning mutagenesis revealed several crucial regions that determine the substrate specificity and catalytic activity. Among the mutants, the S586A variant displayed increased catalytic efficiency and substrate affinity, which is attributed to decreased steric hindrance and increased hydrophobicity, as verified by the saturation mutagenesis at S586. Our results provide structural information about the residues important for the protein engineering of TDC to improve catalytic efficiency in the green manufacturing of tyramine. Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding.,Zhu H, Xu G, Zhang K, Kong X, Han R, Zhou J, Ni Y Sci Rep. 2016 Jun 13;6:27779. doi: 10.1038/srep27779. PMID:27292129 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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