5KXV

Structure Proteinase K at 0.98 Angstroms

5KXV の概要

• エントリーDOI: 10.2210/pdb5kxv/pdb
• 関連するPDBエントリー: 5KXU
• 分子名称: Proteinase K, NITRATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: serine protease, hydrolysis, aminolysis, catalytic triad, hydrolase
• 由来する生物種: Engyodontium album
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29285.14

構造登録者

Masuda, T.,Suzuki, M.,Inoue, S.,Numata, K.,Sugahara, M. (登録日: 2016-07-20, 公開日: 2017-06-07, 最終更新日: 2024-10-23)

主引用文献

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.
Atomic resolution structure of serine protease proteinase K at ambient temperature.
Sci Rep, 7:45604-45604, 2017

PubMed 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.

PubMed: 28361898
DOI: 10.1038/srep45604

実験手法

X-RAY DIFFRACTION (0.98 Å)