3rbl

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Current revision (12:17, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3rbl' size='340' side='right'caption='[[3rbl]], [[Resolution|resolution]] 3.24&Aring;' scene=''>
<StructureSection load='3rbl' size='340' side='right'caption='[[3rbl]], [[Resolution|resolution]] 3.24&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rbl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RBL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rbl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RBL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.24&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rbf|3rbf]], [[3rch|3rch]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AADC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aromatic-L-amino-acid_decarboxylase Aromatic-L-amino-acid decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.28 4.1.1.28] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rbl OCA], [https://pdbe.org/3rbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rbl RCSB], [https://www.ebi.ac.uk/pdbsum/3rbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rbl ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rbl OCA], [https://pdbe.org/3rbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rbl RCSB], [https://www.ebi.ac.uk/pdbsum/3rbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rbl ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/DDC_HUMAN DDC_HUMAN]] Aromatic L-amino acid decarboxylase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/DDC_HUMAN DDC_HUMAN] Aromatic L-amino acid decarboxylase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DDC_HUMAN DDC_HUMAN]] Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.
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[https://www.uniprot.org/uniprot/DDC_HUMAN DDC_HUMAN] Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:22143761</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3rbl" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[DOPA decarboxylase|DOPA decarboxylase]]
*[[DOPA decarboxylase|DOPA decarboxylase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aromatic-L-amino-acid decarboxylase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cellini, B]]
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[[Category: Borri Voltattorni C]]
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[[Category: Cutruzzola, F]]
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[[Category: Cellini B]]
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[[Category: Gianni, S]]
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[[Category: Cutruzzola F]]
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[[Category: Giardina, G]]
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[[Category: Gianni S]]
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[[Category: Montioli, R]]
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[[Category: Giardina G]]
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[[Category: Paiardini, A]]
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[[Category: Montioli R]]
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[[Category: Voltattorni, C Borri]]
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[[Category: Paiardini A]]
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[[Category: Aadc deficiency]]
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[[Category: Apo enzyme]]
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[[Category: Apo form]]
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[[Category: Conformational change]]
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[[Category: Ddc]]
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[[Category: Decarboxylase]]
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[[Category: Exposed]]
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[[Category: L-dopa]]
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[[Category: Lyase]]
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[[Category: Open conformation]]
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[[Category: Open dimer]]
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[[Category: Parkinson]]
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[[Category: Plp]]
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Current revision

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

PDB ID 3rbl

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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