This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3te4

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3te4"

Categories: Drosophila melanogaster | Large Structures | Cheng KC | Huang SH | Lyu PC

@@ Line 3: / Line 3: @@
 <StructureSection load='3te4' size='340' side='right'caption='[[3te4]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<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>
-</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>
+</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>
-<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>
+<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>
 </table>
 == 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;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3te4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Drome]]
+[[Category: Drosophila melanogaster]]
 [[Category: Large Structures]]
-[[Category: Cheng, K C]]
+[[Category: Cheng KC]]
-[[Category: Huang, S H]]
+[[Category: Huang SH]]
-[[Category: Lyu, P C]]
+[[Category: Lyu PC]]
-[[Category: Dopamine/acetyl coa]]
-[[Category: N-acetyltransferase domain]]
-[[Category: Transferase]]

3te4

From Proteopedia

Current revision

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

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox