X-ray structure analysis of human oxidized nucleotide hydrolase MTH1 using crystals obtained under microgravity
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DOI[10.15011//jasma.36.360103]to the data of the same series
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- Material Type
- 記事
- Author/Editor
- Teruya NakamuraKeisuke HirataKana Fujimiya
- Publication, Distribution, etc.
- Publication Date
- 2019-01-31
- Publication Date (W3CDTF)
- 2019-01-31
- Periodical title
- International journal of microgravity science and application : IJMSA
- No. or year of volume/issue
- 36(1)
- Volume
- 36(1)
- ISSN (Periodical Title)
- 2188-9783
- ISSN-L (Periodical Title)
- 0915-3616
- Text Language Code
- eng
- DOI
- 10.15011//jasma.36.360103
- Persistent ID (NDL)
- info:ndljp/pid/11374504
- Collection
- Collection (Materials For Handicapped People:1)
- Collection (particular)
- 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
- Acquisition Basis
- オンライン資料収集制度
- Date Accepted (W3CDTF)
- 2019-10-16T20:43:03+09:00
- Date Captured (W3CDTF)
- 2019-02-22
- Format (IMT)
- application/pdf
- Access Restrictions
- 国立国会図書館内限定公開
- Service for the Digitized Contents Transmission Service
- 図書館・個人送信対象外
- Availability of remote photoduplication service
- 可
- Periodical Title (URI)
- Periodical Title (Persistent ID (NDL))
- info:ndljp/pid/11374499
- Data Provider (Database)
- 国立国会図書館 : 国立国会図書館デジタルコレクション
- Summary, etc.
- 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
- Access Restrictions
- インターネット公開
- Data Provider (Database)
- 科学技術振興機構 : J-STAGE
- Summary, etc.
- 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
- Access Restrictions
- インターネット公開
- Related Material (URI)
- Data Provider (Database)
- 国立情報学研究所 : CiNii Research
- Original Data Provider (Database)
- Japan Link Center雑誌記事索引データベースCiNii Articles科学研究費助成事業データベース科学研究費助成事業データベース科学研究費助成事業データベース
- Bibliographic ID (NDL)
- 11374504
- NAID
- 130007769928