7dai: Difference between revisions
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The | ==The crystal structure of a serotonin N-acetyltransferase from Oryza Sativa== | ||
<StructureSection load='7dai' size='340' side='right'caption='[[7dai]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7dai]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DAI FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=7dai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dai OCA], [https://pdbe.org/7dai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dai RCSB], [https://www.ebi.ac.uk/pdbsum/7dai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dai ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SNAT1_ORYSJ SNAT1_ORYSJ] Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin (PubMed:22998587, PubMed:24134674, PubMed:27121038). Catalyzes in vitro the N-acetylation of tryptamine to produce N-acetyltryptamine, 5-methoxytryptamine to produce melatonin and tyramine to produce N-acetyltyramine (PubMed:27121038). Acetyltransferase required for geminivirus infection and systemic spread (By similarity).[UniProtKB:Q7X9V3]<ref>PMID:22998587</ref> <ref>PMID:24134674</ref> <ref>PMID:27121038</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Serotonin N-acetyltransferase (SNAT) is the key rate-limiting enzyme in melatonin biosynthesis. It mediates melatonin biosynthesis in plants by using serotonin and 5-methoxytryptamine (5-MT), but little is known of its underlying mechanisms. Herein, we present a detailed reaction mechanism of a SNAT from Oryza sativa through combined structural and molecular dynamics (MD) analysis. We report the crystal structures of plant SNAT in the apo and binary/ternary complex forms with acetyl-CoA (AcCoA), serotonin, and 5-MT. OsSNAT exhibits a unique enzymatically active dimeric fold not found in the known structures of arylalkylamine N-acetyltransferase (AANAT) family. The key residues W188, D189, D226, N220, and Y233 located around the active pocket are important in catalysis, confirmed by site-directed mutagenesis. Combined with MD simulations, we hypothesize a novel plausible catalytic mechanism in which D226 and Y233 function as catalytic base and acid during the acetyl-transfer reaction. | |||
Structural and Molecular Dynamics Analysis of Plant Serotonin N-Acetyltransferase Reveal an Acid/Base-Assisted Catalysis in Melatonin Biosynthesis.,Liao L, Zhou Y, Xu Y, Zhang Y, Liu X, Liu B, Chen X, Guo Y, Zeng Z, Zhao Y Angew Chem Int Ed Engl. 2021 May 17;60(21):12020-12026. doi:, 10.1002/anie.202100992. Epub 2021 Apr 7. PMID:33682300<ref>PMID:33682300</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7dai" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Serotonin N-acetyltransferase|Serotonin N-acetyltransferase]] | ||
[[Category: Tang | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Oryza sativa Japonica Group]] | |||
[[Category: Guo Y]] | |||
[[Category: Liao LJ]] | |||
[[Category: Liu B]] | |||
[[Category: Liu XK]] | |||
[[Category: Tang T]] | |||
[[Category: Zhao YC]] | |||
[[Category: Zhou YZ]] | |||
Latest revision as of 19:29, 29 November 2023
The crystal structure of a serotonin N-acetyltransferase from Oryza SativaThe crystal structure of a serotonin N-acetyltransferase from Oryza Sativa
Structural highlights
FunctionSNAT1_ORYSJ Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin (PubMed:22998587, PubMed:24134674, PubMed:27121038). Catalyzes in vitro the N-acetylation of tryptamine to produce N-acetyltryptamine, 5-methoxytryptamine to produce melatonin and tyramine to produce N-acetyltyramine (PubMed:27121038). Acetyltransferase required for geminivirus infection and systemic spread (By similarity).[UniProtKB:Q7X9V3][1] [2] [3] Publication Abstract from PubMedSerotonin N-acetyltransferase (SNAT) is the key rate-limiting enzyme in melatonin biosynthesis. It mediates melatonin biosynthesis in plants by using serotonin and 5-methoxytryptamine (5-MT), but little is known of its underlying mechanisms. Herein, we present a detailed reaction mechanism of a SNAT from Oryza sativa through combined structural and molecular dynamics (MD) analysis. We report the crystal structures of plant SNAT in the apo and binary/ternary complex forms with acetyl-CoA (AcCoA), serotonin, and 5-MT. OsSNAT exhibits a unique enzymatically active dimeric fold not found in the known structures of arylalkylamine N-acetyltransferase (AANAT) family. The key residues W188, D189, D226, N220, and Y233 located around the active pocket are important in catalysis, confirmed by site-directed mutagenesis. Combined with MD simulations, we hypothesize a novel plausible catalytic mechanism in which D226 and Y233 function as catalytic base and acid during the acetyl-transfer reaction. Structural and Molecular Dynamics Analysis of Plant Serotonin N-Acetyltransferase Reveal an Acid/Base-Assisted Catalysis in Melatonin Biosynthesis.,Liao L, Zhou Y, Xu Y, Zhang Y, Liu X, Liu B, Chen X, Guo Y, Zeng Z, Zhao Y Angew Chem Int Ed Engl. 2021 May 17;60(21):12020-12026. doi:, 10.1002/anie.202100992. Epub 2021 Apr 7. PMID:33682300[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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