|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of Drosophila 3,4-dihydroxyphenylalanine decarboxylase== | | ==Crystal structure of Drosophila 3,4-dihydroxyphenylalanine decarboxylase== |
| - | <StructureSection load='3k40' size='340' side='right' caption='[[3k40]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='3k40' size='340' side='right'caption='[[3k40]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3k40]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K40 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K40 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3k40]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K40 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG10697, Ddc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=3k40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k40 OCA], [https://pdbe.org/3k40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k40 RCSB], [https://www.ebi.ac.uk/pdbsum/3k40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k40 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aromatic-L-amino-acid_decarboxylase Aromatic-L-amino-acid decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.28 4.1.1.28] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3k40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k40 OCA], [http://pdbe.org/3k40 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k40 RCSB], [http://www.ebi.ac.uk/pdbsum/3k40 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k40 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DDC_DROME DDC_DROME]] Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine. Variation in the synthesis of bioamines may be a factor contributing to natural variation in life span.<ref>PMID:12881721</ref> | + | [https://www.uniprot.org/uniprot/DDC_DROME DDC_DROME] Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine. Variation in the synthesis of bioamines may be a factor contributing to natural variation in life span.<ref>PMID:12881721</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 34: |
Line 32: |
| | ==See Also== | | ==See Also== |
| | *[[DOPA decarboxylase|DOPA decarboxylase]] | | *[[DOPA decarboxylase|DOPA decarboxylase]] |
| - | *[[User:Brian Hernandez/DOPA Decarboxylase|User:Brian Hernandez/DOPA Decarboxylase]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aromatic-L-amino-acid decarboxylase]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Drome]] | + | [[Category: Large Structures]] |
| - | [[Category: Christensen, B M]] | + | [[Category: Christensen BM]] |
| - | [[Category: Ding, H]] | + | [[Category: Ding H]] |
| - | [[Category: Han, Q]] | + | [[Category: Han Q]] |
| - | [[Category: Li, J]] | + | [[Category: Li J]] |
| - | [[Category: Robinson, H]] | + | [[Category: Robinson H]] |
| - | [[Category: Alpha beta protein]]
| + | |
| - | [[Category: Alternative splicing]]
| + | |
| - | [[Category: Catecholamine biosynthesis]]
| + | |
| - | [[Category: Cg10697-pb isoform b]]
| + | |
| - | [[Category: Decarboxylase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Plp dependent protein]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| - | [[Category: Pyridoxal phosphate]]
| + | |
| Structural highlights
Function
DDC_DROME Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine. Variation in the synthesis of bioamines may be a factor contributing to natural variation in life span.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
BACKGROUND: 3,4-Dihydroxyphenylalanine decarboxylase (DDC), also known as aromatic L-amino acid decarboxylase, catalyzes the decarboxylation of a number of aromatic L-amino acids. Physiologically, DDC is responsible for the production of dopamine and serotonin through the decarboxylation of 3,4-dihydroxyphenylalanine and 5-hydroxytryptophan, respectively. In insects, both dopamine and serotonin serve as classical neurotransmitters, neuromodulators, or neurohormones, and dopamine is also involved in insect cuticle formation, eggshell hardening, and immune responses. PRINCIPAL FINDINGS: In this study, we expressed a typical DDC enzyme from Drosophila melanogaster, critically analyzed its substrate specificity and biochemical properties, determined its crystal structure at 1.75 Angstrom resolution, and evaluated the roles residues T82 and H192 play in substrate binding and enzyme catalysis through site-directed mutagenesis of the enzyme. Our results establish that this DDC functions exclusively on the production of dopamine and serotonin, with no activity to tyrosine or tryptophan and catalyzes the formation of serotonin more efficiently than dopamine. CONCLUSIONS: The crystal structure of Drosophila DDC and the site-directed mutagenesis study of the enzyme demonstrate that T82 is involved in substrate binding and that H192 is used not only for substrate interaction, but for cofactor binding of drDDC as well. Through comparative analysis, the results also provide insight into the structure-function relationship of other insect DDC-like proteins.
Crystal structure and substrate specificity of Drosophila 3,4-dihydroxyphenylalanine decarboxylase.,Han Q, Ding H, Robinson H, Christensen BM, Li J PLoS One. 2010 Jan 21;5(1):e8826. PMID:20098687[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ De Luca M, Roshina NV, Geiger-Thornsberry GL, Lyman RF, Pasyukova EG, Mackay TF. Dopa decarboxylase (Ddc) affects variation in Drosophila longevity. Nat Genet. 2003 Aug;34(4):429-33. PMID:12881721 doi:http://dx.doi.org/10.1038/ng1218
- ↑ Han Q, Ding H, Robinson H, Christensen BM, Li J. Crystal structure and substrate specificity of Drosophila 3,4-dihydroxyphenylalanine decarboxylase. PLoS One. 2010 Jan 21;5(1):e8826. PMID:20098687 doi:10.1371/journal.pone.0008826
|
