Abstract
Hen egg white lysozyme was the first enzyme whose structure was determined by X-ray crystallography1. The proposed mechanism2–4 based on this structure involves the distortion of the saccharide residue (2-acetamido-2-deoxy-D-muramic acid, NAM) in the natural substrate5 (an alternating β(1→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 enzymatic6, chemical17, theoretical8–12, and physical13 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-hydrolysed13 trisaccharide NAM-NAG-NAM bound in subsites B, C, D. Our interpretation of the 2.5-Å resolution difference map does not involve distortion of this residue in site D. Comparison with the structure of the δ-lactone derived from tetra N-acetylchitotetraose ((NAG)3NAL) bound to lysozyme14 suggests we may be looking at a Michaelis complex.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Blake, C. C. F. et al. Nature 206, 757–761 (1965).
Blake, C. C. F., Mair, G. A., North, A. C. T., Phillips, D. C. & Sarma, V. R. Proc. R. Soc. 167, 365–377 (1967).
Blake, C. C. F. et al. Proc. R. Soc. B167, 378–388 (1967).
Phillips, D. C. Sci. Am. 215, 78–90 (1966).
Rupley, J. A. Proc. R. Soc. B167, 416–428 (1967).
Chipman, D. M. Grisaro, V. & Sharon, N. J. biol. Chem. 242, 4388–4394 (1967).
Rand-Meir, T., Dahlquist, F. W. & Raferty, M. A. Biochemistry 8, 4206–4212 (1969).
Levitt, M. in Proceedings of the Rehovot Symposium on Poly (Amino Acids), Polypeptides and Proteins and their Biological Implications (eds Blout, E. R., Bovey, F. A., Goodman, M. & Lotan, N.) 99–113 (Wiley, New York, 1974).
Warshel, A. & Levitt, M. J. molec. Biol. 103, 227–249 (1976).
Vernon, C. A. Proc. R. Soc. B. 167, 389–401 (1967).
Doonan, S., Vernon, C. A. & Banks, B. B. C. Prog. Biophys. molec. Biol. 20, 249 (1970).
Warshel, A. Proc. natn Acad. Sci. U.S.A. 75, 5250–5254 (1978).
Patt, S. L., Baldo, J. H., Boekelheide, K., Weisz, G. & Sykes, B. D. Can. J. Biochem. 56, 624–629 (1978).
Ford, L. O., Johnson, L. N., Machin, P. A., Phillips, D. C. & Tijan, R. J. molec. Biol. 88, 349–371 (1974).
Corey, R. B., Stanford, R. H. Jr, March, R. E., Leung, Y. C. & Kay, L. M. Acta crystallogr. 15, 1157–1163(1962).
Thiessen, W. E. & Levy, H. A. J. appl. Crystallogr. 6, 309 (1973).
Mo, F. & Jensen, L. H. Acta crystallogr. B34, 1562–1569 (1978).
Knox, J. R. & Murthy, N. S. Acta crystallogr. B30, 365–371 (1974).
Brayer, G. D., Delbaere, L. T. J. & James, M. N. G. J. molec. Biol. 124, 243–260 (1978).
North, A. C. T., Phillips, D. C. & Mathews, F. S. Acta crystallogr. A24, 351–359 (1968).
Hendrickson, W. A. J. molec. Biol. 106, 889–893 (1976).
Stewart, J. M., Kundall, F. A. & Baldwin, J. C. The X-Ray-70 System (University of Maryland, College Park, 1970).
Perkins, S. J., Johnson, L. N., Mackin, P. A. & Phillips, D. C. Biochem. J. 173, 607–616 (1978).
Secemski, I. I. Lehrer, S. S. & Lienhard, G. E. J. biol. Chem. 247, 4740–4748 (1972).
Holler, E., Rupley, J. A. & Hess, G. P. Biochemistry 14, 1088–1094 (1975).
Holler, E., Rupley, J. A. & Hess, G. P. Biochemistry 14, 2377–2385 (1975).
Patt, S. L. thesis, Harvard Univ. (1975).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kelly, J., Sielecki, A., Sykes, B. et al. X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme. Nature 282, 875–878 (1979). https://doi.org/10.1038/282875a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/282875a0
This article is cited by
-
Non-statistical assembly of multicomponent [Pd2ABCD] cages
Nature Chemistry (2024)
-
Anti-Inflammatory Effects of Lysozyme Against HMGB1 in Human Endothelial Cells and in Mice
Inflammation (2015)
-
Organic solvents identify specific ligand binding sites on protein surfaces
Nature Biotechnology (1997)
-
Chitinases, chitosanases, and lysozymes can be divided into procaryotic and eucaryotic families sharing a conserved core
Nature Structural Biology (1996)
-
X-ray structure of an anti-fungal chitosanase from streptomyces N174
Nature Structural Biology (1996)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.