High-pressure protein crystallography of hen egg-white lysozyme
Abstract
The crystal structure of hen egg-white lysozyme (HEWL) was analyzed under pressures of up to 950 MPa. The high pressure modified the conformation of the molecule and induced a novel phase transition in the tetragonal crystal of HEWL. Crystal structures of hen egg-white lysozyme (HEWL) determined under pressures ranging from ambient pressure to 950 MPa are presented. From 0.1 to 710 MPa, the molecular and internal cavity volumes are monotonically compressed. However, from 710 to 890 MPa the internal cavity volume remains almost constant. Moreover, as the pressure increases to 950 MPa, the tetragonal crystal of HEWL undergoes a phase transition from P4{sub 3}2{sub 1}2 to P4{sub 3}. Under high pressure, the crystal structure of the enzyme undergoes several local and global changes accompanied by changes in hydration structure. For example, water molecules penetrate into an internal cavity neighbouring the active site and induce an alternate conformation of one of the catalytic residues, Glu35. These phenomena have not been detected by conventional X-ray crystal structure analysis and might play an important role in the catalytic activity of HEWL.
- Authors:
-
- Nagoya University, Chikusa, Nagoya, Aichi 464-8603 (Japan)
- Publication Date:
- OSTI Identifier:
- 22347698
- Resource Type:
- Journal Article
- Journal Name:
- Acta Crystallographica. Section D: Biological Crystallography
- Additional Journal Information:
- Journal Volume: 71; Journal Issue: Pt 4; Other Information: PMCID: PMC4388261; PMID: 25849385; PUBLISHER-ID: mh5172; OAI: oai:pubmedcentral.nih.gov:4388261; Copyright (c) Yamada et al. 2015; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0907-4449
- Country of Publication:
- Denmark
- Language:
- English
- Subject:
- 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; CRYSTALS; HYDRATION; LYSOZYME; MOLECULES; PRESSURE RANGE MEGA PA 10-100; WATER
Citation Formats
Yamada, Hiroyuki, Nagae, Takayuki, Watanabe, Nobuhisa, and Nagoya University, Chikusa, Nagoya, Aichi 464-8603. High-pressure protein crystallography of hen egg-white lysozyme. Denmark: N. p., 2015.
Web. doi:10.1107/S1399004715000292.
Yamada, Hiroyuki, Nagae, Takayuki, Watanabe, Nobuhisa, & Nagoya University, Chikusa, Nagoya, Aichi 464-8603. High-pressure protein crystallography of hen egg-white lysozyme. Denmark. https://doi.org/10.1107/S1399004715000292
Yamada, Hiroyuki, Nagae, Takayuki, Watanabe, Nobuhisa, and Nagoya University, Chikusa, Nagoya, Aichi 464-8603. 2015.
"High-pressure protein crystallography of hen egg-white lysozyme". Denmark. https://doi.org/10.1107/S1399004715000292.
@article{osti_22347698,
title = {High-pressure protein crystallography of hen egg-white lysozyme},
author = {Yamada, Hiroyuki and Nagae, Takayuki and Watanabe, Nobuhisa and Nagoya University, Chikusa, Nagoya, Aichi 464-8603},
abstractNote = {The crystal structure of hen egg-white lysozyme (HEWL) was analyzed under pressures of up to 950 MPa. The high pressure modified the conformation of the molecule and induced a novel phase transition in the tetragonal crystal of HEWL. Crystal structures of hen egg-white lysozyme (HEWL) determined under pressures ranging from ambient pressure to 950 MPa are presented. From 0.1 to 710 MPa, the molecular and internal cavity volumes are monotonically compressed. However, from 710 to 890 MPa the internal cavity volume remains almost constant. Moreover, as the pressure increases to 950 MPa, the tetragonal crystal of HEWL undergoes a phase transition from P4{sub 3}2{sub 1}2 to P4{sub 3}. Under high pressure, the crystal structure of the enzyme undergoes several local and global changes accompanied by changes in hydration structure. For example, water molecules penetrate into an internal cavity neighbouring the active site and induce an alternate conformation of one of the catalytic residues, Glu35. These phenomena have not been detected by conventional X-ray crystal structure analysis and might play an important role in the catalytic activity of HEWL.},
doi = {10.1107/S1399004715000292},
url = {https://www.osti.gov/biblio/22347698},
journal = {Acta Crystallographica. Section D: Biological Crystallography},
issn = {0907-4449},
number = Pt 4,
volume = 71,
place = {Denmark},
year = {Wed Apr 01 00:00:00 EDT 2015},
month = {Wed Apr 01 00:00:00 EDT 2015}
}