TY - JOUR
T1 - Structural basis for the broad range substrate specificity of a novel mouse cytosolic sulfotransferase-mSULT1D1
AU - Teramoto, Takamasa
AU - Sakakibara, Yoichi
AU - Liu, Ming Cheh
AU - Suiko, Masahito
AU - Kimura, Makoto
AU - Kakuta, Yoshimitsu
N1 - Funding Information:
This research was supported by the Grant-in-Aid for Scientific Research and the National Project on Protein Structural and Functional Analyses from the Ministry of Education, Culture, Sports, Science and Technology, Japan.
PY - 2009/1/30
Y1 - 2009/1/30
N2 - The mouse cytosolic sulfotransferase, mSULT1D1, catalyzes the sulfonation of a wide range of phenolic molecules including p-nitrophenol (pNP), α-naphthol (αNT), serotonin, as well as dopamine and its metabolites. To gain insight into the structural basis for its broad range substrate specificity, we solved two distinct ternary crystal structures of mSULT1D1, complexed with 3′-phosphoadenosine-5′-phosphate (PAP) plus pNP or PAP plus αNT. The structures revealed that the mSULT1D1 contains an L-shaped accepter-binding site which comprises 20 amino acid residues and four conserved water molecules. The shape of the accepter-binding site can be adjusted by conformational changes of two residues, Ile148 and Glu247, upon binding with respective substrates.
AB - The mouse cytosolic sulfotransferase, mSULT1D1, catalyzes the sulfonation of a wide range of phenolic molecules including p-nitrophenol (pNP), α-naphthol (αNT), serotonin, as well as dopamine and its metabolites. To gain insight into the structural basis for its broad range substrate specificity, we solved two distinct ternary crystal structures of mSULT1D1, complexed with 3′-phosphoadenosine-5′-phosphate (PAP) plus pNP or PAP plus αNT. The structures revealed that the mSULT1D1 contains an L-shaped accepter-binding site which comprises 20 amino acid residues and four conserved water molecules. The shape of the accepter-binding site can be adjusted by conformational changes of two residues, Ile148 and Glu247, upon binding with respective substrates.
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U2 - 10.1016/j.bbrc.2008.12.013
DO - 10.1016/j.bbrc.2008.12.013
M3 - Article
C2 - 19073143
AN - SCOPUS:58149468347
SN - 0006-291X
VL - 379
SP - 76
EP - 80
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -