3AW7

Crystal structure of tetragonal hen egg white lysozyme at 71.9% relative humidity

3AW7 の概要

• エントリーDOI: 10.2210/pdb3aw7/pdb
• 関連するPDBエントリー: 3AW6
• 分子名称: Lysozyme C, ACETATE ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14471.64

構造登録者

Takayama, Y.,Nakasako, M. (登録日: 2011-03-11, 公開日: 2011-03-30, 最終更新日: 2024-10-16)

主引用文献

Takayama, Y.,Nakasako, M.
A few low-frequency normal modes predominantly contribute to conformational responses of hen egg white lysozyme in the tetragonal crystal to variations of molecular packing controlled by environmental humidity
Biophys.Chem., 159:237-246, 2011

PubMed Abstract: The structures of proteins in crystals are fixed by molecular interactions with neighboring molecules, except in non-contacting flexible regions. Thus, it is difficult to imagine what conformational changes occur in solution. However, if molecular interactions can be changed by manipulating molecular packing in crystals, it may be possible to visualize conformational responses of proteins at atomic resolution by diffraction experiments. For this purpose, it is suitable to control the molecular packing in protein crystals by changing the volume of solvent channels through variation of the environmental relative humidity. Here, we studied conformational responses of hen egg white lysozyme (HEWL) in the tetragonal crystal by X-ray diffraction experiments using a humidity-control apparatus, which provided air flow of 20-98%rh at 298 K. First, we monitored the lattice parameters and crystalline order during dehydration and rehydration of HEWL crystal between 61 and 94%rh at 300 K. Then two crystal structures at a resolution of 2.1 Å using diffraction data obtained at 84.2 and 71.9%rh were determined to discuss the conformational responses of HEWL against the external perturbation induced by changes in molecular packing. The structure at 71.9%rh displayed a closure movement that was likely induced by the molecular contacts formed during dehydration and could be approximated by ten low-frequency normal modes for the crystal structure obtained at 84.2%rh. In addition, we observed reorganization of hydration structures at the molecular interfaces between symmetry neighbors. These findings suggest that humidity-controlled X-ray crystallography is an effective tool to investigate the responses of inherent intramolecular motions of proteins to external perturbations.

PubMed: 21802827
DOI: 10.1016/j.bpc.2011.07.001

実験手法

X-RAY DIFFRACTION (2.1 Å)