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Article Abstract
We determined the crystal structure of a LysM module from Pteris ryukyuensis chitinase-A (PrLysM2) at a resolution of 1.8 Å. Structural and binding analysis of PrLysM2 indicated that this module recognizes chitin oligosaccharides in a shallow groove comprised of five sugar-binding subsites on one side of the molecule. The free energy changes (ΔG°) for binding of (GlcNAc), (GlcNAc), and (GlcNAc) to PrLysM2 were determined to be -5.4, -5,4 and -4.6 kcal mol, respectively, by ITC. Thermodynamic dissection of the binding energetics of (GlcNAc) revealed that the driving force is the enthalpy change (ΔH° = -11.7 ± 0.2 kcal/mol) and the solvation entropy change (-TΔS° = -5.9 ± 0.6 kcal/mol). This is the first description of thermodynamic signatures of a chitin oligosaccharide binding to a LysM module.
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