1b6b

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1b6b, resolution 2.5Å

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

Overview

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.

About this Structure

1B6B is a Single protein structure of sequence from Ovis aries. Active as Aralkylamine N-acetyltransferase, with EC number 2.3.1.87 Full crystallographic information is available from OCA.

Reference

Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism., Hickman AB, Klein DC, Dyda F, Mol Cell. 1999 Jan;3(1):23-32. PMID:10024876

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