X-ray structure analysis of human oxidized nucleotide hydrolase MTH1 using crystals obtained under microgravity

• 資料種別: 記事
• タイトル: X-ray structure analysis of human oxidized nucleotide hydrolase MTH1 using crystals obtained under microgravity
• 著者・編者: Teruya Nakamura; Keisuke Hirata; Kana Fujimiya
• 出版事項: 日本 : 日本マイクログラビティ応用学会
• 出版年月日等: 2019-01-31
• 出版年（W3CDTF）: 2019-01-31
• タイトル（掲載誌）: International journal of microgravity science and application : IJMSA
• 巻号年月日等（掲載誌）: 36(1)
• 掲載巻: 36(1)
• ISSN（掲載誌）: 2188-9783
• ISSN-L（掲載誌）: 0915-3616
• 本文の言語コード: eng
• DOI: 10.15011//jasma.36.360103; https://doi.org/10.15011//jasma.36.360103
• 国立国会図書館永続的識別子: info:ndljp/pid/11374504; https://dl.ndl.go.jp/pid/11374504
• コレクション（共通）: 障害者向け資料
• コレクション（障害者向け資料：レベル1）: テキストデータ
• コレクション（個別）: 国立国会図書館デジタルコレクション > 電子書籍・電子雑誌 > 学術機関 > 学協会; https://dl.ndl.go.jp/collections/B00043
• 収集根拠: オンライン資料収集制度
• 受理日（W3CDTF）: 2019-10-16T20:43:03+09:00
• 保存日（W3CDTF）: 2019-02-22
• 記録形式（IMT）: application/pdf
• オンライン閲覧公開範囲: 国立国会図書館内限定公開
• デジタル化資料送信: 図書館・個人送信対象外
• 遠隔複写可否（NDL）: 可
• 掲載誌（URI）: https://www.jasma.info/journal/archives/report/x-ray-structure-analysis-of-human-oxidized-nucleotide-hydrolase-mth1-using-crystals-obtained-under-microgravity
• 掲載誌（国立国会図書館永続的識別子）: info:ndljp/pid/11374499; https://dl.ndl.go.jp/pid/11374499
• 連携機関・データベース: 国立国会図書館 : 国立国会図書館デジタルコレクション; https://dl.ndl.go.jp

• 要約等: 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.
• DOI: 10.15011//jasma.36.360103
• オンライン閲覧公開範囲: インターネット公開
• 連携機関・データベース: 科学技術振興機構 : J-STAGE; http://www.jstage.jst.go.jp

• 要約等: 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.
• DOI: 10.15011//jasma.36.360103; https://doi.org/10.15011//jasma.36.360103
• オンライン閲覧公開範囲: インターネット公開
• 関連情報（URI）: http://id.ndl.go.jp/digimeta/11374504; https://dl.ndl.go.jp/pid/11374504
• 連携機関・データベース: 国立情報学研究所 : CiNii Research; https://cir.nii.ac.jp/
• 提供元機関・データベース: Japan Link Center; https://japanlinkcenter.org/top; 雑誌記事索引データベース; https://ndlsearch.ndl.go.jp; CiNii Articles; 科学研究費助成事業データベース; https://kaken.nii.ac.jp/ja
• 書誌ID（NDLBibID）: 11374504; http://id.ndl.go.jp/bib/11374504
• NII論文ID: 130007769928