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

Proceedings of the National Academy of Sciences of the United States of America, ISSN: 0027-8424
2011
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Dataset Description

Experimental Technique/Method:X-RAY DIFFRACTION Resolution:3.24 Classification:LYASE Release Date:2011-10-19 Deposition Date:2011-03-29 Revision Date:2012-01-04 Molecular Weight:107961.84 Macromolecule Type:Protein Residue Count:960 Atom Site Count:6950 DOI:10.2210/pdb3rbl/pdb Abstract: 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 Å 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 conformati...

Bibliographic Details

Giardina G.; Montioli R.; Gianni S.; Cellini B.; Paiardini A.; Voltattorni C.B.; Cutruzzola F.; Giardina, G.; Montioli, R.; Gianni, S.; Cellini, B.; Paiardini, A.; Borri Voltattorni, C.; Cutruzzola, F.

Worldwide Protein Data Bank

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