3RBF: Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the apo form

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.
PDB ID: 3RBFDownload
MMDB ID: 94465
PDB Deposition Date: 2011/3/29
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.9  Å
Source Organism:
Similar Structures:
Biological Unit for 3RBF: dimeric; determined by author and by software (PISA)
Molecular Components in 3RBF
Label Count Molecule
Proteins (2 molecules)
Aromatic-l-amino-acid Decarboxylase
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

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