Crystal structure of human catecholamine sulfotransferase

Bidwell, Lisa M., McManus, Michael E., Gaedigk, Andrea, Kakuta, Yoshimitsu, Negishi, Masa, Pedersen, Lars and Martin, Jennifer L. (1999) Crystal structure of human catecholamine sulfotransferase. Journal of Molecular Biology, 293 3: 521-530. doi:10.1006/jmbi.1999.3153

Author Bidwell, Lisa M.
McManus, Michael E.
Gaedigk, Andrea
Kakuta, Yoshimitsu
Negishi, Masa
Pedersen, Lars
Martin, Jennifer L.
Title Crystal structure of human catecholamine sulfotransferase
Journal name Journal of Molecular Biology   Check publisher's open access policy
ISSN 0022-2836
Publication date 1999-10-29
Sub-type Article (original research)
DOI 10.1006/jmbi.1999.3153
Volume 293
Issue 3
Start page 521
End page 530
Total pages 10
Editor Peter Wright
Place of publication London, UK
Publisher Academic Press
Collection year 1999
Language eng
Subject C1
270108 Enzymes
780105 Biological sciences
Formatted abstract
Sulfonation, like phosphorylation, can modify the activity of a variety of biological molecules. The sulfotransferase enzymes sulfonate neurotransmitters, drugs, steroid hormones, dietary carcinogens and proteins. SULT1A3 specifically sulfonates catecholamines such as dopamine, adrenaline and noradrenaline. The crystal structure of SULT1A3 with a sulfate bound at the active site, has been determined at 2.4 Å resolution. Although the core α/β fold is like that of estrogen and heparan sulfotransferases, major differences occur in and around the active site. Most notably, several regions surrounding the active site, including a section of 40 residues, are disordered in SULT1A3. Regions that are topologically equivalent to the disordered parts of SULT1A3 are involved in substrate and cofactor binding in estrogen and heparan sulfotransferase. Flexibility in these regions suggests that ligand binding elicits a disorder-order transition in and around the active site of sulfotransferases and might contribute to the broad substrate specificity of these enzymes.
© 1999 Academic Press
Keyword Biochemistry & Molecular Biology
Protein Structure
Flavonol 3-sulfotransferase
Phenol Sulfotransferase
Mutational Analysis
Protein Models
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Faculty of Science Publications
School of Medicine Publications
School of Pharmacy Publications
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Citation counts: TR Web of Science Citation Count  Cited 80 times in Thomson Reuters Web of Science Article | Citations
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Created: Tue, 10 Jun 2008, 15:11:54 EST