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X-ray stru...

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

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

Persistent ID (NDL)
info:ndljp/pid/11374504
Material type
記事
Author
Teruya Nakamuraほか
Publisher
日本マイクログラビティ応用学会
Publication date
2019-01-31
Material Format
Digital
Journal name
International journal of microgravity science and application : IJMSA 36(1)
Publication Page
-
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Summary, etc.:

Human MTH1 hydrolyzes oxidized nucleoside triphosphates with broad substrate specificity and draws attention as a potential anticancer target. Recentl...

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Digital

Material Type
記事
Author/Editor
Teruya Nakamura
Keisuke Hirata
Kana Fujimiya
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
Persistent ID (NDL)
info:ndljp/pid/11374504
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
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

Digital

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

Digital

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.
Access Restrictions
インターネット公開
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