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Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase
Author(s) -
Teramoto Takamasa,
Sakakibara Yoichi,
Inada Kanako,
Kurogi Katsuhisa,
Liu Ming-Cheh,
Suiko Masahito,
Kimura Makoto,
Kakuta Yoshimitsu
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.10.035
Subject(s) - dopamine , catecholamine , chemistry , biochemistry , cytosol , sulfotransferase , enzyme , biology , endocrinology
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.