Abstract
CELLULOSE is the major polysaccharide component of plant cell walls and is the most abundant organic compound on the planet. A number of bacterial1 and fungal2 organisms can use cellulose as a food source, possessing cellulases (cellobiohydrolases and endoglucanases) that can catalyse the hydrolysis of the β-(1,4) glycosidic bonds. They can be classified into seven distinct families3. The three-dimensional structures of members of two of these families are known4,5. Here we report the structure of a third cellulase, endoglucanase V, whose sequence is not represented in any of the above families. The enzyme is structurally distinct from the previously determined cellulases but is similar to a recently characterized plant defence protein6. The active site region resembles that of lysozyme, despite the lack of structural similarity between these two enzymes.
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Davies, G., Dodson, G., Hubbard, R. et al. Structure and function of endoglucanase V. Nature 365, 362–364 (1993). https://doi.org/10.1038/365362a0
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DOI: https://doi.org/10.1038/365362a0
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