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1efh

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(New page: 200px<br /> <applet load="1efh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1efh, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 14:36, 12 November 2007

Image:1efh.gif

1efh, resolution 2.40Å

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CRYSTAL STRUCTURE OF THE HUMAN HYDROXYSTEROID SULFOTRANSFERASE IN THE PRESENCE OF PAP

Contents

Overview

The crystal structure of SULT2A3 human hydroxysteroid sulfotransferase has, been solved at 2.4 A resolution in the presence of 3'-phosphoadenosine, 5'-phosphate (PAP). The overall structure is similar to those of SULT1, enzymes such as estrogen sulfotransferase and the PAP binding site is, conserved, however, significant differences exist in the positions of, loops Pro14-Ser20, Glu79-Ile82 and Tyr234-Gln244 in the substrate binding, pocket. Moreover, protein interaction in the crystal structure has, revealed a possible dimer-directed conformational alteration that may, regulate the SULT activity.

Disease

Known diseases associated with this structure: Histidinemia OMIM:[609457], Selective T-cell defect OMIM:[176947]

About this Structure

1EFH is a Single protein structure of sequence from Homo sapiens with A3P as ligand. Active as Alcohol sulfotransferase, with EC number 2.8.2.2 Full crystallographic information is available from OCA.

Reference

Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase., Pedersen LC, Petrotchenko EV, Negishi M, FEBS Lett. 2000 Jun 9;475(1):61-4. PMID:10854859

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