Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase.
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 alpha/beta domain with a five-stranded parallel beta-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.
Teramoto
Takamasa
T
Laboratory of Structural Biology, Department of Systems Life Sciences, Japan.
Sakakibara
Yoichi
Y
Inada
Kanako
K
Kurogi
Katsuhisa
K
Liu
Ming-Cheh
MC
Suiko
Masahito
M
Kimura
Makoto
M
Kakuta
Yoshimitsu
Y
D000595:Amino Acid Sequence; D000818:Animals; D015239:Arylsulfotransferase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004252:DNA Mutational Analysis; D004298:Dopamine / Q000378:metabolism*; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary / Q000235:genetics; D015238:Sulfotransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
C431463:SULT1D1 sulfotransferase; D015238:Sulfotransferases; D015239:Arylsulfotransferase; D004298:Dopamine