1CJW

SEROTONIN N-ACETYLTRANSFERASE COMPLEXED WITH A BISUBSTRATE ANALOG

1CJW の概要

• エントリーDOI: 10.2210/pdb1cjw/pdb
• 分子名称: PROTEIN (SEROTONIN N-ACETYLTRANSFERASE), COA-S-ACETYL TRYPTAMINE (3 entities in total)
• 機能のキーワード: n-acetyl transferase, transferase
• 由来する生物種: Ovis aries (sheep)
• 細胞内の位置: Cytoplasm (By similarity): Q29495
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19602.15

構造登録者

Hickman, A.B.,Namboodiri, M.A.A.,Klein, D.C.,Dyda, F. (登録日: 1999-04-19, 公開日: 1999-05-06, 最終更新日: 2023-08-09)

主引用文献

Hickman, A.B.,Namboodiri, M.A.,Klein, D.C.,Dyda, F.
The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog.
Cell(Cambridge,Mass.), 97:361-369, 1999

PubMed Abstract: Serotonin N-acetyltransferase, a member of the GNAT acetyltransferase superfamily, is the penultimate enzyme in the conversion of serotonin to melatonin, the circadian neurohormone. Comparison of the structures of the substrate-free enzyme and the complex with a bisubstrate analog, coenzyme A-S-acetyltryptamine, demonstrates that acetyl coenzyme A (AcCoA) binding is accompanied by a large conformational change that in turn leads to the formation of the serotonin-binding site. The structure of the complex also provides insight into how the enzyme may facilitate acetyl transfer. A water-filled channel leading from the active site to the surface provides a pathway for proton removal following amine deprotonation. Furthermore, structural and mutagenesis results indicate an important role for Tyr-168 in catalysis.

PubMed: 10319816
DOI: 10.1016/S0092-8674(00)80745-X

実験手法

X-RAY DIFFRACTION (1.8 Å)