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, Yoshimitsu Kakuta

研究成果: ジャーナルへの寄稿記事

25 引用 (Scopus)

抄録

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 S N 2-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.

元の言語英語
記事番号1572
ジャーナルNature communications
4
DOI
出版物ステータス出版済み - 4 11 2013

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sulfation
tyrosine
Tyrosine
Crystal structure
proteins
Protein Isoforms
crystal structure
peptides
Peptides
Proteins
Complement C4
L Forms
Complement C3
Receptor Protein-Tyrosine Kinases
Post Translational Protein Processing
Catalysis
Substrates
complement
catalysis
enzymes

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

これを引用

Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction. / Teramoto, Takamasa; Fujikawa, Yukari; Kawaguchi, Yoshirou; Kurogi, Katsuhisa; Soejima, Masayuki; Adachi, Rumi; Nakanishi, Yuichi; Mishiro-Sato, Emi; Liu, Ming Cheh; Sakakibara, Yoichi; Suiko, Masahito; Kimura, Makoto; Kakuta, Yoshimitsu.

:: Nature communications, 巻 4, 1572, 11.04.2013.

研究成果: ジャーナルへの寄稿記事

Teramoto, T, Fujikawa, Y, Kawaguchi, Y, Kurogi, K, Soejima, M, Adachi, R, Nakanishi, Y, Mishiro-Sato, E, Liu, MC, Sakakibara, Y, Suiko, M, Kimura, M & Kakuta, Y 2013, 'Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction', Nature communications, 巻. 4, 1572. https://doi.org/10.1038/ncomms2593
Teramoto, Takamasa ; Fujikawa, Yukari ; Kawaguchi, Yoshirou ; Kurogi, Katsuhisa ; Soejima, Masayuki ; Adachi, Rumi ; Nakanishi, Yuichi ; Mishiro-Sato, Emi ; Liu, Ming Cheh ; Sakakibara, Yoichi ; Suiko, Masahito ; Kimura, Makoto ; Kakuta, Yoshimitsu. / Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction. :: Nature communications. 2013 ; 巻 4.
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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 {\AA} resolution. Structural and complementary mutational analyses revealed the molecular basis for catalysis being an S N 2-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.",
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AU - Nakanishi, Yuichi

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