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Human Sulfotranferase 1A1 (hSULT1A1) catalyzes the transfer of a sulforyl group from a 3’-phosphoadenosine 5’-phosphosulfate (PAPS) donor to a variety of substrates (acceptors) containing either an amine or a hydroxyl group, leading to modification of the acceptor’s biological activity. In order to gain insight into the molecular mechanism underlying the broad specificity of hSULT1A1, we have crystallized the enzyme and determined its structure in the presence of 3’ phosphoadenosine 5’-phosphate (PAP) alone, PAP and 3-Cyano-7-Coumarin (3CyC), and PAP and 2-Napthol (2NAP). These structures demonstrated high plasticity of the acceptor binding site which was mainly attributed to substantial movements of the gating loop (residues 86-90) that enabled the binding of large and elongated phenol substrates. We were also interested in increasing the SULT1A1 specificity to para-nitrophenol (pNP) on the account of the other substrates through the use of directed evolution methodology. This method allowed the generation of a hSULT1A1 variant mutated at position D249G which exhibits a marked increase in activity toward pNP while decreasing its activity toward 3CyC and 2NAP. The determined crystal structure of D249G revealed the effect of the mutation on surface electrostatic potential and loop stability in the proximity of the active site pocket.

Crystal structures of human sulfotransferase 1A1: from broad to narrow specificity