7dal

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The crystal structure of a serotonin N-acetyltransferase in complex with serotonin and acetyl-CoA from Oryza Sativa

Structural highlights

7dal is a 2 chain structure with sequence from Oryza sativa Japonica Group. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:ACO, SRO
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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][1] [2] [3]

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[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. ↑ Kang K, Lee K, Park S, Byeon Y, Back K. Molecular cloning of rice serotonin N-acetyltransferase, the penultimate gene in plant melatonin biosynthesis. J Pineal Res. 2013 Aug;55(1):7-13. doi: 10.1111/jpi.12011. Epub 2012 Sep 24. PMID:22998587 doi:http://dx.doi.org/10.1111/jpi.12011
  2. ↑ Byeon Y, Lee HY, Lee K, Park S, Back K. Cellular localization and kinetics of the rice melatonin biosynthetic enzymes SNAT and ASMT. J Pineal Res. 2014 Jan;56(1):107-14. doi: 10.1111/jpi.12103. Epub 2013 Nov 12. PMID:24134674 doi:http://dx.doi.org/10.1111/jpi.12103
  3. ↑ Byeon Y, Lee HY, Back K. Cloning and characterization of the serotonin N-acetyltransferase-2 gene (SNAT2) in rice (Oryza sativa). J Pineal Res. 2016 Sep;61(2):198-207. doi: 10.1111/jpi.12339. Epub 2016 May 22. PMID:27121038 doi:http://dx.doi.org/10.1111/jpi.12339
  4. ↑ Liao L, Zhou Y, Xu Y, Zhang Y, Liu X, Liu B, Chen X, Guo Y, Zeng Z, Zhao Y. Structural and Molecular Dynamics Analysis of Plant Serotonin N-Acetyltransferase Reveal an Acid/Base-Assisted Catalysis in Melatonin Biosynthesis. Angew Chem Int Ed Engl. 2021 May 17;60(21):12020-12026. doi:, 10.1002/anie.202100992. Epub 2021 Apr 7. PMID:33682300 doi:http://dx.doi.org/10.1002/anie.202100992

Contents


PDB ID 7dal

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OCA

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