7DAJ

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

7DAJ の概要

• エントリーDOI: 10.2210/pdb7daj/pdb
• 分子名称: Serotonin N-acetyltransferase 1, chloroplastic, ACETYL COENZYME *A (3 entities in total)
• 機能のキーワード: n-acetyltransferase, transferase
• 由来する生物種: Oryza sativa subsp. japonica (Rice)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38633.42

構造登録者

Zhou, Y.Z.,Liao, L.J.,Tang, T.,Guo, Y.,Liu, X.K.,Liu, B.,Zhao, Y.C. (登録日: 2020-10-16, 公開日: 2021-09-22, 最終更新日: 2023-11-29)

主引用文献

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., 60:12020-12026, 2021

PubMed Abstract: 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.

PubMed: 33682300
DOI: 10.1002/anie.202100992

実験手法

X-RAY DIFFRACTION (2.3 Å)