Lysozyme With Asp 52 Replaced By Ser 52

Entry retrieved from the Protein Data Bank at RCSB.

1LSZ: Hydrolase(O-Glycosyl). Date: Sep 27, 1994
Authors: A.T.Hadfield, D.J.Harvey, D.B.Archer, D.A.Mackenzie, D.J.Jeenes, S.E.Radford, G.Lowe, C.M.Dobson, L.N.Johnson
Compound: Lysozyme (E.C.3.2.1.17) Mutant With Asp 52 Replaced By Ser (D52s)
Ligand: Complexed With Glcnac4 (Tetra-N-Acetyl Chitotetraose), NAG
Source: Hen (Gallus Gallus) Egg White Recombinant Form.
Method: X-Ray Diffraction. Resolution: 2.0 Ang.

Lysozyme is an enzyme that facilitates the destruction of cell walls that are composed of alternating NAM (N-acetylmuramic acid) and NAG (N-acetylglucosamine) units. Lysozyme does so by way of electrostatic catalysis of NAM-NAG bond cleavage. Asp 52 and Glu 35 are key to the catalytic action. In the present structure, Asp 52 has been replaced by Ser 52. If the discussed mechanism of electrostatic catalysis of lysozyme is correct, then this modified lysozyme should be much less efficient than the actual lysozyme. Ser 52 and Glu 35 are shown in spacefill. Find Ser 52 and Glu 35 in the binding pocket.


Figure. The X-ray structure of egg white lysozyme with Asp 52 replaced by Ser 52.