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On the similar spatial arrangement of active site residues in PAPS-dependent and phenolic sulfate-utilizing sulfotransferases |
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| Authors: | Takamasa Teramoto Rumi Adachi Ming-Cheh Liu Makoto Kimura Yoshimitsu Kakuta |
| Institution: | a Laboratory of Structural Biology, Department of Systems Life Sciences, Graduate School, Faculty of Agriculture, Kyushu University, Hakozaki 6-10-1, Higashi-ku, Fukuoka 812-8581, Japan b Venture Business Laboratory, Kyushu University, Hakozaki 6-10-1, Higashi-ku, Fukuoka 812-8581, Japan c Laboratory of Applied Biochemistry, Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, University of Miyazaki, Miyazaki 889-2192, Japan d Department of Pharmacology, College of Pharmacy, The University of Toledo, Toledo, OH 43606, USA e Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University, Hakozaki 6-10-1, Higashi-ku, Fukuoka 812-8581, Japan |
| Abstract: | Mammalian sulfotransferases (STs) utilize exclusively the sulfuryl group donor 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to catalyze the sulfurylation reactions based on a sequential transfer mechanism. In contrast, the commensal intestinal bacterial arylsulfate sulfotransferases (ASSTs) do not use PAPS as the sulfuryl group donor, but instead catalyze sulfuryl transfer from phenolic sulfate to a phenol via a Ping-Pong mechanism. Interestingly, structural comparison revealed a similar spatial arrangement of the active site residues as well as the cognate substrates in mouse ST (mSULT1D1) and Escherichia coli CFT073 ASST, despite that their overall structures bear no discernible relationship. These observations suggest that the active sites of PAPS-dependent SULT1D1 and phenolic sulfate-utilizing ASST represent an example of convergent evolution. |
| Keywords: | Convergent evolution Sulfotransferase X-ray crystallography |
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