Atomic resolution structure of serine protease proteinase K at ambient temperature

Tetsuya Masuda, Mamoru Suzuki, Shigeyuki Inoue, Changyong Song, Takanori Nakane, Eriko Nango, Rie Tanaka, Kensuke Tono, Yasumasa Joti, Takashi Kameshima, Takaki Hatsui, Makina Yabashi, Bunzo Mikami, Osamu Nureki, Keiji Numata, So Iwata, Michihiro Sugahara

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10 Citations (Scopus)

Abstract

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.

Original languageEnglish
Article number45604
JournalScientific reports
Volume7
DOIs
Publication statusPublished - 2017 Mar 31

ASJC Scopus subject areas

  • General

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    Masuda, T., Suzuki, M., Inoue, S., Song, C., Nakane, T., Nango, E., Tanaka, R., Tono, K., Joti, Y., Kameshima, T., Hatsui, T., Yabashi, M., Mikami, B., Nureki, O., Numata, K., Iwata, S., & Sugahara, M. (2017). Atomic resolution structure of serine protease proteinase K at ambient temperature. Scientific reports, 7, [45604]. https://doi.org/10.1038/srep45604