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- Title
Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase
- Authors
Teramoto, Takamasa; Sakakibara, Yoichi; Inada, Kanako; Kurogi, Katsuhisa; Liu, Ming-Cheh; Suiko, Masahito; Kimura, Makoto; Kakuta, Yoshimitsu
- Abstract
Abstract: 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.
- Subjects
SULFOTRANSFERASES; CRYSTALLOGRAPHY; DOPAMINE; HOMEOSTASIS; CATECHOLAMINES; SULFONATION; LABORATORY mice
- Publication
FEBS Letters, 2008, Vol 582, Issue 28, p3909
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2008.10.035