3rch | pdb_00003rch

Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the open conformation with LLP and PLP bound to Chain-A and Chain-B respectively

spinqualitylabelsall models 3rch, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rch is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PLP NonStd Res: LLP Related: 3rbf, 3rbl Gene: AADC (HUMAN) Activity: Aromatic-L-amino-acid decarboxylase, with EC number 4.1.1.28 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [DDC_HUMAN] Aromatic L-amino acid decarboxylase deficiency. The disease is caused by mutations affecting the gene represented in this entry. Function [DDC_HUMAN] Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine. Publication Abstract from PubMed DOPA decarboxylase, the dimeric enzyme responsible for the synthesis of neurotransmitters dopamine and serotonin, is involved in severe neurological diseases such as Parkinson disease, schizophrenia, and depression. Binding of the pyridoxal-5'-phosphate (PLP) cofactor to the apoenzyme is thought to represent a central mechanism for the regulation of its activity. We solved the structure of the human apoenzyme and found it exists in an unexpected open conformation: compared to the pig kidney holoenzyme, the dimer subunits move 20 A apart and the two active sites become solvent exposed. Moreover, by tuning the PLP concentration in the crystals, we obtained two more structures with different conformations of the active site. Analysis of three-dimensional data coupled to a kinetic study allows to identify the structural determinants of the open/close conformational change occurring upon PLP binding and thereby propose a model for the preferential degradation of the apoenzymes of Group II decarboxylases. Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases.,Giardina G, Montioli R, Gianni S, Cellini B, Paiardini A, Voltattorni CB, Cutruzzola F Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20514-9. Epub 2011 Dec 5. PMID:22143761 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also DOPA decarboxylase

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