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We have biochemically and structurally characterized a novel glucanase from the less studied GH64 family in a bacterium significant for fermentation of carbohydrates into biofuels. This enzyme displays a peculiar property of being distally modulated by Ca2+ via assistance from a neighboring βγ-crystallin domain, likely through changes in the domain interface. In addition, this enzyme is found to be optimized for functioning in an acidic environment, which is in line with the possibility of its involvement in biofuel production. Multiple occurrences of a similar domain architecture suggest that such a “βγ-crystallination”-mediated Ca2+ sensitivity may be widespread among bacterial proteins.

βγ-Crystallination Endows a Novel Bacterial Glycoside Hydrolase 64 with Ca 2+ -Dependent Activity Modulation

βγ-Crystallination Endows a Novel Bacterial Glycoside Hydrolase 64 with Ca ²⁺ -Dependent Activity Modulation