The identification by X-ray crystallography of the site of attachment of an affinity label to hen egg-white lysozyme

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Abstract

Tetragonal crystals of hen egg-white lysozyme were treated with the active sitedirected irreversible inhibitor 2′,3′epoxypropyl β-glycoside of N-acetyl-d-glucosamine, β(1→4)-linked dimer. The crystals were examined by X-ray crystallography, and the results compared to those obtained from crystals of the reversible complex formed between hen egg-white lysozyme and the β-phenyl glycoside of GlcNAc β(1→4)GlcNAc. It is concluded that the GlcNAc β(1→4)GlcNAc moiety of the irreversible inhibitor occupies subsites B and C in the active site of the enzyme, and that the inhibitor is linked covalently to the enzyme through the carboxyl side-chain of Asp 52. © 1973.

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Moult, J., Eshdat, Y., & Sharon, N. (1973). The identification by X-ray crystallography of the site of attachment of an affinity label to hen egg-white lysozyme. Journal of Molecular Biology, 75(1). https://doi.org/10.1016/0022-2836(73)90524-X

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