4XEN

High pressure protein crystallography of hen egg white lysozyme in complex with Tetra-N-acetylchitotetraose at 920 MPa

Summary for 4XEN

• Entry DOI: 10.2210/pdb4xen/pdb
• Related: 4wld 4wlt 4wlx 4wly 4wm1 4wm2 4wm3 4wm4 4wm5 4wm6
• Descriptor: Lysozyme C, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SODIUM ION, ... (5 entities in total)
• Functional Keywords: hydrolase
• Biological source: Gallus gallus (Chicken)
• Total number of polymer chains: 1
• Total formula weight: 15326.75

Authors

Yamada, H.,Watanabe, N.,Nagae, T. (deposition date: 2014-12-24, release date: 2015-04-08, Last modification date: 2024-11-06)

Primary citation

Yamada, H.,Nagae, T.,Watanabe, N.
High-pressure protein crystallography of hen egg-white lysozyme
Acta Crystallogr.,Sect.D, 71:742-753, 2015

PubMed Abstract: 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 P43212 to P43. 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.

PubMed: 25849385
DOI: 10.1107/S1399004715000292

Experimental method

X-RAY DIFFRACTION (1.55 Å)