X-ray Structure Analysis of Human Oxidized Nucleotide Hydrolase MTH1 using Crystals Obtained under Microgravity

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  • NAKAMURA Teruya
    Priority Organization for Innovation and Excellence, Kumamoto University Graduate School of Pharmaceutical Sciences, Kumamoto University
  • HIRATA Keisuke
    Graduate School of Pharmaceutical Sciences, Kumamoto University
  • FUJIMIYA Kana
    School of Pharmacy, Kumamoto University
  • CHIRIFU Mami
    Graduate School of Pharmaceutical Sciences, Kumamoto University
  • ARIMORI Takao
    Institute for Protein Research, Osaka University
  • TAMADA Taro
    Quantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology
  • IKEMIZU Shinji
    Graduate School of Pharmaceutical Sciences, Kumamoto University
  • YAMAGATA Yuriko
    Graduate School of Pharmaceutical Sciences, Kumamoto University

書誌事項

公開日
2019
資源種別
journal article
DOI
  • 10.15011//jasma.36.360103
公開者
日本マイクログラビティ応用学会

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説明

Human MTH1 hydrolyzes oxidized nucleoside triphosphates with broad substrate specificity and draws attention as a potential anticancer target. Recently, we determined the high resolution crystal structures of MTH1 and suggested that MTH1 recognizes different substrates via an exchange of the protonation state at Asp119 and Asp120. In order to validate this mechanism, it is essential to observe hydrogen atoms by ultra-high resolution X-ray crystallography and/or neutron crystallography using large high quality crystals. Here we carried out the crystallization of MTH1 in complex with a substrate, 8-oxo-dGTP, under microgravity in the Japanese Experiment Module ‘Kibo’. One of the crystals diffracted to 1.04-Å resolution, which is better than that we reported previously. We carried out bond length analysis of Asp119 and Asp120 using this updated data, which revealed the protonation state based on the bond lengths with higher accuracy and precision.

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