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タイトル: Atomic resolution structure of serine protease proteinase K at ambient temperature.
著者: Masuda, Tetsuya
Suzuki, Mamoru
Inoue, Shigeyuki
Song, Changyong
Nakane, Takanori
Nango, Eriko
Tanaka, Rie
Tono, Kensuke
Joti, Yasumasa
Kameshima, Takashi
Hatsui, Takaki
Yabashi, Makina
Mikami, Bunzo
Nureki, Osamu
Numata, Keiji
Iwata, So  kyouindb  KAKEN_id
Sugahara, Michihiro
著者名の別形: 桝田, 哲哉
鈴木, 守
登野,健介
岩田, 想
菅原, 道泰
発行日: 31-Mar-2017
出版者: Springer Nature
誌名: Scientific reports
巻: 7
論文番号: 45604
抄録: Atomic resolution structures (beyond 1.20 Å) at ambient temperature, which is usually hampered by the radiation damage in synchrotron X-ray crystallography (SRX), will add to our understanding of the structure-function relationships of enzymes. Serial femtosecond crystallography (SFX) has attracted surging interest by providing a route to bypass such challenges. Yet the progress on atomic resolution analysis with SFX has been rather slow. In this report, we describe the 1.20 Å resolution structure of proteinase K using 13 keV photon energy. Hydrogen atoms, water molecules, and a number of alternative side-chain conformations have been resolved. The increase in the value of B-factor in SFX suggests that the residues and water molecules adjacent to active sites were flexible and exhibited dynamic motions at specific substrate-recognition sites.
記述: 酵素の立体構造、「SACLA」のX線レーザーを用いて常温、原子分解能構造解析に成功--体内に近い環境での酵素反応機構解明から、新薬や機能性分子創生に期待--. 京都大学プレスリリース. 2017-04-07.
著作権等: © The Author(s) 2017. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
URI: http://hdl.handle.net/2433/219505
DOI(出版社版): 10.1038/srep45604
PubMed ID: 28361898
関連リンク: http://www.kyoto-u.ac.jp/ja/research/research_results/2016/170331_1.html
出現コレクション:学術雑誌掲載論文等

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