Abstract
The structure of endoglucanase I (EG I) from Trichoderma reesei has been investigated in solution, using small-angle x-ray scattering. The enzyme showed the typical shape (“tadpole”) and domain arrangement (catalytic core-spacer-cellulose binding domain) which is obviously common to all celluloses degrading solid substrate. The molecular size parameters resemble cellobiohydrolase I closely: radius of gyration is 4.74 nm, overall length 18.0 nm, diameter 5.3 nm. The main difference lies in the spacer region, which contains much more scattering mass, probably due to a higher extent of glycosylation which extends towards the core domain.
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© 1993 Dr. Dietrich Steinkopff Verlag GmbH & Co. KG
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Abuja, P.P., Hayn, M., Chen, H., Esterbauer, H. (1993). The structure of endoglucanase I (Trichoderma resei) in solution. In: Laggner, P., Glatter, O. (eds) Trends in Colloid and Interface Science VII. Progress in Colloid & Polymer Science, vol 93. Steinkopff. https://doi.org/10.1007/BFb0118500
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DOI: https://doi.org/10.1007/BFb0118500
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