1B6B

MELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSFERASE AT 2.5 A RESOLUTION SUGGESTS A CATALYTIC MECHANISM

1B6B の概要

• エントリーDOI: 10.2210/pdb1b6b/pdb
• 分子名称: PROTEIN (ARYLALKYLAMINE N-ACETYLTRANSFERASE) (2 entities in total)
• 機能のキーワード: acetyltransferase, 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: 2
• 化学式量合計: 39112.95

構造登録者

Hickman, A.B.,Klein, D.C.,Dyda, F. (登録日: 1999-01-13, 公開日: 2000-01-14, 最終更新日: 2023-12-27)

主引用文献

Hickman, A.B.,Klein, D.C.,Dyda, F.
Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism.
Mol.Cell, 3:23-32, 1999

PubMed Abstract: Conversion of serotonin to N-acetylserotonin, the precursor of the circadian neurohormone melatonin, is catalyzed by serotonin N-acetyltransferase (AANAT) in a reaction requiring acetyl coenzyme A (AcCoA). AANAT is a globular protein consisting of an eight-stranded beta sheet flanked by five alpha helices; a conserved motif in the center of the beta sheet forms the cofactor binding site. Three polypeptide loops converge above the AcCoA binding site, creating a hydrophobic funnel leading toward the cofactor and serotonin binding sites in the protein interior. Two conserved histidines not found in other NATs are located at the bottom of the funnel in the active site, suggesting a catalytic mechanism for acetylation involving imidazole groups acting as general acid/base catalysts.

PubMed: 10024876
DOI: 10.1016/S1097-2765(00)80171-9

実験手法

X-RAY DIFFRACTION (2.5 Å)