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.
|Number of pages||5|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - Jan 30 2009|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology