9LYZ

X-RAY CRYSTALLOGRAPHY OF THE BINDING OF THE BACTERIAL CELL WALL TRISACCHARIDE NAM-NAG-NAM TO LYSOZYME

Summary for 9LYZ

• Entry DOI: 10.2210/pdb9lyz/pdb
• Related: 6LYZ
• Descriptor: HEN EGG WHITE LYSOZYME, N-acetyl-beta-muramic acid-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-N-acetyl-beta-muramic acid (3 entities in total)
• Functional Keywords: hydrolase (o-glycosyl)
• Biological source: GALLUS GALLUS (CHICKEN)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 15102.88

Authors

Kelly, J.A.,James, M.N.G. (deposition date: 1979-12-06, release date: 1980-02-27, Last modification date: 2024-10-23)

Primary citation

Kelly, J.A.,Sielecki, A.R.,Sykes, B.D.,James, M.N.,Phillips, D.C.
X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme.
Nature, 282:875-878, 1979

PubMed Abstract: Hen egg white lysozyme was the first enzyme whose structure was determined by X-ray crystallography. The proposed mechanism based on this structure involves the distortion of the saccharide residue (2-acetamido-2-deoxy-D-muramic acid, NAM) in the natural substrate (an alternating beta (1 leads to 4) linked oligomer of 2-acetamido-2-deoxy-D-glucose (NAG) and NAM residues) bound to site D in the binding cleft. The importance of substrate distortion has prompted numerous enzymatic, chemical, theoretical, and physical studies, but there is little direct crystallographic evidence on the conformation of a NAM residue bound at site D. We now present the X-ray structure of the non-hydrolysed trisaccharide NAM-NAG-NAM bound in subsites B, C, D. Our interpretation of the 2.5-A resolution difference map does not involve distortion of this residue in site D. Comparison with the structure of the delta-lactone derived from tetra N-acetylchitotetraose (NAG)3NAL) bound to lysozyme suggests we may be looking at a Michaelis complex.

PubMed: 514367
DOI: 10.1038/282875a0

Experimental method

X-RAY DIFFRACTION (2.5 Å)