PDBsum entry 4xen

Hydrolase

PDB id: 4xen

Contents

Protein chain

129 a.a.

Ligands

NAG-NAG-NAG-NAG

Metals

_CL ×4

_NA

Waters ×172

PDB id:

4xen

Name:

Hydrolase

Title:

High pressure protein crystallography of hen egg white lysozyme in complex with tetra-n-acetylchitotetraose at 920 mpa

Structure:

LysozymE C. Chain: a. Fragment: unp residues 19-147. Synonym: 1,4-beta-n-acetylmuramidasE C,allergen gal d iv. Ec: 3.2.1.17

Source:

Gallus gallus. Chicken. Organism_taxid: 9031

Resolution:

1.55Å R-factor: 0.167 R-free: 0.210

Authors:

H.Yamada,N.Watanabe,T.Nagae

Key ref:

H.Yamada et al. (2015). High-pressure protein crystallography of hen egg-white lysozyme. Acta Crystallogr D Biol Crystallogr, 71, 742-753. PubMed id: 25849385 DOI: 10.1107/S1399004715000292

Date:

24-Dec-14 Release date: 08-Apr-15

Protein chain

P00698  (LYSC_CHICK) -  Lysozyme C from Gallus gallus

Seq: 147 a.a.

Struc: 129 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.17 - lysozyme.
• Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

DOI no: 10.1107/S1399004715000292

Acta Crystallogr D Biol Crystallogr 71:742-753 (2015)

PubMed id: 25849385

High-pressure protein crystallography of hen egg-white lysozyme.

H.Yamada, T.Nagae, N.Watanabe.

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.