3te4

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Current revision (08:37, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3te4' size='340' side='right'caption='[[3te4]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
<StructureSection load='3te4' size='340' side='right'caption='[[3te4]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3te4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TE4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3te4]] is a 1 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=3TE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TE4 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=ACO:ACETYL+COENZYME+*A'>ACO</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]] 1.46&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG3318, Dat, Dmel_CG3318 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=ACO:ACETYL+COENZYME+*A'>ACO</scene></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=3te4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te4 OCA], [https://pdbe.org/3te4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3te4 RCSB], [https://www.ebi.ac.uk/pdbsum/3te4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3te4 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=3te4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te4 OCA], [https://pdbe.org/3te4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3te4 RCSB], [https://www.ebi.ac.uk/pdbsum/3te4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3te4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DNAT_DROME DNAT_DROME]] Catalyzes N-acetylation of tryptamine, tyramine, dopamine, serotonin and octopamine. Is not essential for sclerotization.<ref>PMID:8901578</ref> <ref>PMID:9703021</ref> <ref>PMID:7498465</ref>
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[https://www.uniprot.org/uniprot/DNAT_DROME DNAT_DROME] Catalyzes N-acetylation of tryptamine, tyramine, dopamine, serotonin and octopamine. Is not essential for sclerotization.<ref>PMID:8901578</ref> <ref>PMID:9703021</ref> <ref>PMID:7498465</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The daily cycle of melatonin biosynthesis in mammals is regulated by arylalkylamine N-acetyltransferase (EC 2.3.1.87, AANAT), making it an attractive target for therapeutic control of abnormal melatonin production in mood and sleep disorders. Drosophila melanogaster dopamine N-acetyltransferase (Dat) is an AANAT. Until this report, no insect Dat structure had been solved, and consequently, the structural basis for its acetyl-transfer activity was not well understood. We report herein the high-resolution crystal structure for a D. melanogaster Dat/acetyl coenzyme A (AcCoA) complex obtained using one-edge (Selenium) single-wavelength anomalous diffraction. The binding study by isothermal titration calorimetry suggested that the cofactor bound to Dat first before substrate. Examination of the complex structure and a substrate-docked model indicated that Dat contains a novel AANAT catalytic triad. A site-directed mutagenesis, a kinetic study and pH&shy;&shy;-rate profiles confirmed that Glu47, Ser182, and Ser186 were critical for catalysis. Collectively, our results suggest that Dat possesses a specialized active site structure dedicated to a catalytic mechanism.
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Crystal Structure of Dopamine N-Acetyltransferase/Acetyl Coenzyme A Complex Provide Insights into the Catalytic Mechanism.,Cheng KC, Liao JN, Lyu PC Biochem J. 2012 Jun 21. PMID:22716280<ref>PMID:22716280</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 3te4" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Drome]]
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[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cheng, K C]]
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[[Category: Cheng KC]]
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[[Category: Huang, S H]]
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[[Category: Huang SH]]
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[[Category: Lyu, P C]]
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[[Category: Lyu PC]]
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[[Category: Dopamine/acetyl coa]]
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[[Category: N-acetyltransferase domain]]
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[[Category: Transferase]]
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Current revision

Crystal structure of dopamine N Acetyltransferase in complex with acetyl-COA from Drosophila Melanogaster

PDB ID 3te4

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