5gi9: Difference between revisions

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== 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>  
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
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Latest revision as of 12:12, 20 March 2024

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

5gi9 is a 1 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DNAT_DROME Catalyzes N-acetylation of tryptamine, tyramine, dopamine, serotonin and octopamine. Is not essential for sclerotization.[1] [2] [3]

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

5gi9, resolution 1.40Å

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OCA
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