Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1

Shinnosuke Tanaka, Toshiaki Nishiyori, Hidetaka Kojo, Reo Otsubo, Moe Tsuruta, Katsuhisa Kurogi, Ming Cheh Liu, Masahito Suiko, Yoichi Sakakibara, Yoshimitsu Kakuta

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19 Citations (Scopus)


Tyrosylprotein sulfotransferases (TPSTs) are enzymes that catalyze post-translational tyrosine sulfation of proteins. In humans, there are only two TPST isoforms, designated TPST1 and TPST2. In a previous study, we reported the crystal structure of TPST2, which revealed the catalytic mechanism of the tyrosine sulfation reaction. However, detailed molecular mechanisms underlying how TPSTs catalyse a variety of substrate proteins with different efficiencies and how TPSTs catalyze the sulfation of multiple tyrosine residues in a substrate protein remain unresolved. Here, we report two crystal structures of the human TPST1 complexed with two substrate peptides that are catalysed by human TPST1 with significantly different efficiencies. The distinct binding modes found in the two complexes provide insight into the sulfation mechanism for these substrates. The present study provides valuable information describing the molecular mechanism of post-translational protein modifications catalysed by TPSTs.

Original languageEnglish
Article number8776
JournalScientific reports
Issue number1
Publication statusPublished - Dec 1 2017

All Science Journal Classification (ASJC) codes

  • General


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