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Figure 3
The effect of mutations of the four solvent-exposed aromatic residues on the hydrolytic activity and binding affinity. (a) The four aromatic residues, highlighted in cyan on the surface of OfChtI-CAD, form a plane to anchor the plane of the crystalline chitin. A model of chitin is shown in orange. (b) The relative hydrolytic activities of the OfChtI-CAD mutants for pNP-(GlcNAc)2 and crystalline α-chitin compared with wild-type OfChtI-CAD. (c) The decrease in free protein concentration after binding of the wild-type and mutant OfChtI-CADs to crystalline α-chitin was determined at different time points over 18 h.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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