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

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)3909-3914
Number of pages6
JournalFEBS Letters
Issue number28
Publication statusPublished - Nov 26 2008

All Science Journal Classification (ASJC) codes

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


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