On the similar spatial arrangement of active site residues in PAPS-dependent and phenolic sulfate-utilizing sulfotransferases.
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.
Teramoto
Takamasa
T
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.
Adachi
Rumi
R
Sakakibara
Yoichi
Y
Liu
Ming-Cheh
MC
Suiko
Masahito
M
Kimura
Makoto
M
Kakuta
Yoshimitsu
Y
D000818:Animals; D015239:Arylsulfotransferase / Q000737:chemistry* / Q000235:genetics; D002384:Catalysis; D020134:Catalytic Domain; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics; D019143:Evolution, Molecular; D051379:Mice; D010724:Phosphoadenosine Phosphosulfate / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D015238:Sulfotransferases
D029968:Escherichia coli Proteins; D010724:Phosphoadenosine Phosphosulfate; C431463:SULT1D1 sulfotransferase; D015238:Sulfotransferases; D015239:Arylsulfotransferase; C090707:arylsulfate sulfotransferase