Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase

Takamasa Teramoto, Yoichi Sakakibara, Kanako Inada, Katsuhisa Kurogi, Ming Cheh Liu, Masahito Suiko, Makoto Kimura, Yoshimitsu Kakuta

研究成果: Contribution to journalArticle

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In mammals, sulfonation as mediated by specific cytosolic sulfotransferases (SULTs) plays an important role in the homeostasis of dopamine and other catecholamines. To gain insight into the structural basis for dopamine recognition/binding, we determined the crystal structure of a mouse dopamine-sulfating SULT, mouse SULT1D1 (mSULT1D1). Data obtained indicated that mSULT1D1 comprises of a single α/β domain with a five-stranded parallel β-sheet. In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. These results imply differences in substrate binding between dopamine-sulfating SULTs from different species.

元の言語英語
ページ(範囲)3909-3914
ページ数6
ジャーナルFEBS Letters
582
発行部数28
DOI
出版物ステータス出版済み - 11 26 2008

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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    Teramoto, T., Sakakibara, Y., Inada, K., Kurogi, K., Liu, M. C., Suiko, M., Kimura, M., & Kakuta, Y. (2008). Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase. FEBS Letters, 582(28), 3909-3914. https://doi.org/10.1016/j.febslet.2008.10.035