Abstract
Abstract The binding of a proposed transition-state analogue, the δ-lactone derived from tetra-N-acetylchitotetraose, to lysozyme in the crystal at pH 2.6 has been studied by X-ray diffraction techniques to a resolution of 2.5 A. The tetrasaccharide lactone is bound in sites A, B, C, D with sugar residues located in sites A, B and C in similar positions to those observed previously in the complex with tri-N-acetylchitotriose. Analysis of the electron density map for site D, by direct model-building and with a computer model-building programme, indicates that the δ-lactone ring is in a conformation close to a sofa or a boat which brings the hydroxymethyl group C(6)O(6) axial. These studies provide support for the role of strain in the proposed mechanism of lysozyme catalysis. The orientation of the lactone group in site D is slightly different from that originally derived by hypothetical model-building.
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