2a3r

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spinqualitylabelsall models 2a3r, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Human Sulfotransferase SULT1A3 in Complex with Dopamine and 3-Phosphoadenosine 5-Phosphate

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The human sulfotransferase, SULT1A3, catalyzes specifically the, sulfonation of monoamines such as dopamine, epinephrine, and, norepinephrine. SULT1A3 also has a unique 3,4-dihydroxyphenylalanine, (Dopa)/tyrosine-sulfating activity that is preferentially toward their, D-form enantiomers and can be stimulated dramatically by Mn2+. To further, our understanding of the molecular basis for the unique substrate, specificity of this enzyme, we solved the crystal structure of human, SULT1A3, complexed with dopamine and 3'-phosphoadenosine 5'-phosphate, at, 2.6 A resolution and carried out autodocking analysis with D-Dopa. The, structure of SULT1A3 enzyme-ligand complex clearly showed that residue, Glu146 can form electrostatic interaction with dopamine and may play a, pivotal role in the stereoselectivity and sulfating activity. On the other, hand, residue Asp86 appeared to be critical to the Mn2+-stimulation of the, Dopa/tyrosine-sulfating activity of SULT1A3, in addition to a supporting, role in the stereoselectivity and sulfating activity.

Disease

Known diseases associated with this structure: Alzheimer disease-4 OMIM:[600759], Cardiomyopathy, dilated, 1V OMIM:[600759]

About this Structure

2A3R is a Single protein structure of sequence from Homo sapiens with A3P and LDP as ligands. Active as Aryl sulfotransferase, with EC number 2.8.2.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3'-phosphoadenosine 5'-phosphate., Lu JH, Li HT, Liu MC, Zhang JP, Li M, An XM, Chang WR, Biochem Biophys Res Commun. 2005 Sep 23;335(2):417-23. PMID:16083857

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