Crystal structure of human catecholamine sulfotransferase

Lisa M. Bidwell, Michael E. McManus, Andrea Gaedigk, Yoshimitsu Kakuta, Masa Negishi, Lars Pedersen, Jennifer L. Martin

研究成果: ジャーナルへの寄稿学術誌査読

99 被引用数 (Scopus)


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.

ジャーナルJournal of Molecular Biology
出版ステータス出版済み - 10月 29 1999

!!!All Science Journal Classification (ASJC) codes

  • 構造生物学
  • 分子生物学


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