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| | <StructureSection load='5gi5' size='340' side='right'caption='[[5gi5]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='5gi5' size='340' side='right'caption='[[5gi5]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gi5]] 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=5GI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GI5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gi5]] 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=5GI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GI5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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]] 1.45Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5gi6|5gi6]], [[5gi7|5gi7]], [[5gi8|5gi8]], [[5gi9|5gi9]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> |
| - | <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'>[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'>[https://proteopedia.org/fgij/fg.htm?mol=5gi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gi5 OCA], [https://pdbe.org/5gi5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gi5 RCSB], [https://www.ebi.ac.uk/pdbsum/5gi5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gi5 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=5gi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gi5 OCA], [https://pdbe.org/5gi5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gi5 RCSB], [https://www.ebi.ac.uk/pdbsum/5gi5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gi5 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>
| + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aralkylamine N-acetyltransferase]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Drome]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cheng, H C]] | + | [[Category: Cheng HC]] |
| - | [[Category: Lyu, P C]] | + | [[Category: Lyu PC]] |
| - | [[Category: Yang, Y C]] | + | [[Category: Yang YC]] |
| - | [[Category: Order bi-bi sequential mechanism]]
| + | |
| - | [[Category: Transferase]]
| + | |
| 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 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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hintermann E, Grieder NC, Amherd R, Brodbeck D, Meyer UA. Cloning of an arylalkylamine N-acetyltransferase (aaNAT1) from Drosophila melanogaster expressed in the nervous system and the gut. Proc Natl Acad Sci U S A. 1996 Oct 29;93(22):12315-20. PMID:8901578
- ↑ Brodbeck D, Amherd R, Callaerts P, Hintermann E, Meyer UA, Affolter M. Molecular and biochemical characterization of the aaNAT1 (Dat) locus in Drosophila melanogaster: differential expression of two gene products. DNA Cell Biol. 1998 Jul;17(7):621-33. PMID:9703021
- ↑ Hintermann E, Jeno P, Meyer UA. Isolation and characterization of an arylalkylamine N-acetyltransferase from Drosophila melanogaster. FEBS Lett. 1995 Nov 13;375(1-2):148-50. PMID:7498465
- ↑ Wu CY, Hu IC, Yang YC, Ding WC, Lai CH, Lee YZ, Liu YC, Cheng HC, Lyu PC. An essential role of acetyl coenzyme A in the catalytic cycle of insect arylalkylamine N-acetyltransferase. Commun Biol. 2020 Aug 14;3(1):441. doi: 10.1038/s42003-020-01177-9. PMID:32796911 doi:http://dx.doi.org/10.1038/s42003-020-01177-9
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