Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8296032 | Biochemical and Biophysical Research Communications | 2017 | 32 Pages |
Abstract
We determined the crystal structure of a LysM module from Pteris ryukyuensis chitinase-A (PrLysM2) at a resolution of 1.8Â Ã
. 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 (ÎGr°) for binding of (GlcNAc)6, (GlcNAc)5, and (GlcNAc)4 to PrLysM2 were determined to be â5.4, â5,4 and â4.6 kcal molâ1, respectively, by ITC. Thermodynamic dissection of the binding energetics of (GlcNAc)6 revealed that the driving force is the enthalpy change (ÎHr° = â11.7 ± 0.2 kcal/mol) and the solvation entropy change (âTÎSsolv° = â5.9 ± 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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Authors
Takayuki Ohnuma, Toki Taira, Naoyuki Umemoto, Yoshihito Kitaoku, Morten Sørlie, Tomoyuki Numata, Tamo Fukamizo,