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==Crystal Structure of Drosophila melanogaster Dopamine N-Acetyltransferase in Ternary Complex with CoA and Acetyl-Tryptamine== | ==Crystal Structure of Drosophila melanogaster Dopamine N-Acetyltransferase in Ternary Complex with CoA and Acetyl-Tryptamine== | ||
<StructureSection load='5gi9' size='340' side='right' caption='[[5gi9]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='5gi9' size='340' side='right'caption='[[5gi9]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5gi9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5gi9]] 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=5GI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GI9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7AN:~{N}-[2-(1~{H}-indol-3-yl)ethyl]ethanamide'>7AN</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=D1D:(4S,5S)-1,2-DITHIANE-4,5-DIOL'>D1D</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7AN:~{N}-[2-(1~{H}-indol-3-yl)ethyl]ethanamide'>7AN</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=D1D:(4S,5S)-1,2-DITHIANE-4,5-DIOL'>D1D</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gi5|5gi5]], [[5gi6|5gi6]], [[5gi7|5gi7]], [[5gi8|5gi8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5gi5|5gi5]], [[5gi6|5gi6]], [[5gi7|5gi7]], [[5gi8|5gi8]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dat, NAT1, CG3318 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dat, NAT1, CG3318 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aralkylamine_N-acetyltransferase Aralkylamine N-acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.87 2.3.1.87] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gi9 OCA], [https://pdbe.org/5gi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gi9 RCSB], [https://www.ebi.ac.uk/pdbsum/5gi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gi9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[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> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Acetyl coenzyme A (Ac-CoA)-dependent N-acetylation is performed by arylalkylamine N-acetyltransferase (AANAT) and is important in many biofunctions. AANAT catalyzes N-acetylation through an ordered sequential mechanism in which cofactor (Ac-CoA) binds first, with substrate binding afterward. No ternary structure containing AANAT, cofactor, and substrate was determined, meaning the details of substrate binding and product release remain unclear. Here, two ternary complexes of dopamine N-acetyltransferase (Dat) before and after N-acetylation were solved at 1.28 A and 1.36 A resolution, respectively. Combined with the structures of Dat in apo form and Ac-CoA bound form, we addressed each stage in the catalytic cycle. Isothermal titration calorimetry (ITC), crystallography, and nuclear magnetic resonance spectroscopy (NMR) were utilized to analyze the product release. Our data revealed that Ac-CoA regulates the conformational properties of Dat to form the catalytic site and substrate binding pocket, while the release of products is facilitated by the binding of new Ac-CoA. | |||
An essential role of acetyl coenzyme A in the catalytic cycle of insect arylalkylamine N-acetyltransferase.,Wu CY, Hu IC, Yang YC, Ding WC, Lai CH, Lee YZ, Liu YC, Cheng HC, Lyu PC Commun Biol. 2020 Aug 14;3(1):441. doi: 10.1038/s42003-020-01177-9. PMID:32796911<ref>PMID:32796911</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5gi9" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 18: | Line 27: | ||
[[Category: Aralkylamine N-acetyltransferase]] | [[Category: Aralkylamine N-acetyltransferase]] | ||
[[Category: Drome]] | [[Category: Drome]] | ||
[[Category: Large Structures]] | |||
[[Category: Cheng, H C]] | [[Category: Cheng, H C]] | ||
[[Category: Cheng, K C]] | [[Category: Cheng, K C]] | ||
Revision as of 13:01, 7 July 2021
Crystal Structure of Drosophila melanogaster Dopamine N-Acetyltransferase in Ternary Complex with CoA and Acetyl-TryptamineCrystal Structure of Drosophila melanogaster Dopamine N-Acetyltransferase in Ternary Complex with CoA and Acetyl-Tryptamine
Structural highlights
Function[DNAT_DROME] Catalyzes N-acetylation of tryptamine, tyramine, dopamine, serotonin and octopamine. Is not essential for sclerotization.[1] [2] [3] Publication Abstract from PubMedAcetyl coenzyme A (Ac-CoA)-dependent N-acetylation is performed by arylalkylamine N-acetyltransferase (AANAT) and is important in many biofunctions. AANAT catalyzes N-acetylation through an ordered sequential mechanism in which cofactor (Ac-CoA) binds first, with substrate binding afterward. No ternary structure containing AANAT, cofactor, and substrate was determined, meaning the details of substrate binding and product release remain unclear. Here, two ternary complexes of dopamine N-acetyltransferase (Dat) before and after N-acetylation were solved at 1.28 A and 1.36 A resolution, respectively. Combined with the structures of Dat in apo form and Ac-CoA bound form, we addressed each stage in the catalytic cycle. Isothermal titration calorimetry (ITC), crystallography, and nuclear magnetic resonance spectroscopy (NMR) were utilized to analyze the product release. Our data revealed that Ac-CoA regulates the conformational properties of Dat to form the catalytic site and substrate binding pocket, while the release of products is facilitated by the binding of new Ac-CoA. An essential role of acetyl coenzyme A in the catalytic cycle of insect arylalkylamine N-acetyltransferase.,Wu CY, Hu IC, Yang YC, Ding WC, Lai CH, Lee YZ, Liu YC, Cheng HC, Lyu PC Commun Biol. 2020 Aug 14;3(1):441. doi: 10.1038/s42003-020-01177-9. PMID:32796911[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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