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Type A Carbohydrate-Binding Modules (CBMs) are a critical component of cellulose-degrading microbial enzymes, but their mechanism of action remains poorly understood. A library of recombinant type A CBMs in fusion with green fluorescent protein was constructed and their binding to cellulose and chitin was characterized over a wide range of temperatures, pHs and ionic strengths. The structure of S. thermophila StCBM64C was further solved, revealing an untwisted, flat, carbohydrate-binding interface comprising the side chains of four tryptophan residues in a coplanar linear arrangement.

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This page is a summary of: Stability and ligand promiscuity of type A carbohydrate-binding modules are illustrated by the structure of Spirochaeta thermophila StCBM64C, Journal of Biological Chemistry, February 2017, American Society for Biochemistry & Molecular Biology (ASBMB), DOI: 10.1074/jbc.m116.767541.
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