Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction

Takamasa Teramoto, Yukari Fujikawa, Yoshirou Kawaguchi, Katsuhisa Kurogi, Masayuki Soejima, Rumi Adachi, Yuichi Nakanishi, Emi Mishiro-Sato, Ming-Cheh Liu, Yoichi Sakakibara, Masahito Suiko, Makoto Kimura and Yoshimitsu Kakuta ()
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Takamasa Teramoto: Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Yukari Fujikawa: Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Yoshirou Kawaguchi: Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Katsuhisa Kurogi: Food Research Branch, Faculty of Agriculture, University of Miyazaki
Masayuki Soejima: Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Rumi Adachi: Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Yuichi Nakanishi: Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Emi Mishiro-Sato: Food Research Branch, Faculty of Agriculture, University of Miyazaki
Ming-Cheh Liu: College of Pharmacy and Pharmaceutical Sciences, The University of Toledo
Yoichi Sakakibara: Food Research Branch, Faculty of Agriculture, University of Miyazaki
Masahito Suiko: Food Research Branch, Faculty of Agriculture, University of Miyazaki
Makoto Kimura: Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Yoshimitsu Kakuta: Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University

Nature Communications, 2013, vol. 4, issue 1, 1-9

Abstract: Abstract Post-translational protein modification by tyrosine sulfation has an important role in extracellular protein–protein interactions. The protein tyrosine sulfation reaction is catalysed by the Golgi enzyme called the tyrosylprotein sulfotransferase. To date, no crystal structure is available for tyrosylprotein sulfotransferase. Detailed mechanism of protein tyrosine sulfation reaction has thus remained unclear. Here we present the first crystal structure of the human tyrosylprotein sulfotransferase isoform 2 complexed with a substrate peptide (C4P5Y3) derived from complement C4 and 3′-phosphoadenosine-5′-phosphate at 1.9 Å resolution. Structural and complementary mutational analyses revealed the molecular basis for catalysis being an SN2-like in-line displacement mechanism. Tyrosylprotein sulfotransferase isoform 2 appeared to recognize the C4 peptide in a deep cleft by using a short parallel β-sheet type interaction, and the bound C4P5Y3 forms an L-shaped structure. Surprisingly, the mode of substrate peptide recognition observed in the tyrosylprotein sulfotransferase isoform 2 structure resembles that observed for the receptor type tyrosine kinases.

Date: 2013
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DOI: 10.1038/ncomms2593

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