4WM6
High pressure protein crystallography of hen egg white lysozyme at 950 MPa
Summary for 4WM6
| Entry DOI | 10.2210/pdb4wm6/pdb |
| Descriptor | Lysozyme C, SODIUM ION (3 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Gallus gallus (Chicken) |
| Total number of polymer chains | 4 |
| Total formula weight | 57416.60 |
| Authors | Yamada, H.,Watanabe, N.,Nagae, T. (deposition date: 2014-10-08, release date: 2015-04-08, Last modification date: 2024-10-30) |
| 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 Cited by 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: 25849385DOI: 10.1107/S1399004715000292 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
Download full validation report
