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-Structure paper
Title | Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases. |
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Journal, issue, pages | Proc. Natl. Acad. Sci. USA, Vol. 108, Page 20514-20519, Year 2011 |
Publish date | Mar 29, 2011 (structure data deposition date) |
![]() | Giardina, G. / Montioli, R. / Gianni, S. / Cellini, B. / Paiardini, A. / Voltattorni, C.B. / Cutruzzola, F. |
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Methods | X-ray diffraction |
Resolution | 2.8 - 3.24 Å |
Structure data | ![]() PDB-3rbf: ![]() PDB-3rbl: ![]() PDB-3rch: |
Chemicals | ![]() ChemComp-PLP: ![]() ChemComp-CL: ![]() ChemComp-HOH: |
Source |
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![]() | LYASE / apo enzyme / apo form / open conformation / open dimer / exposed / conformational change / Parkinson / AADC deficiency / DDC / Decarboxylase / PLP binding / PLP / L-DOPA / LLP / internal aldimine / Shiff Base |