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The structure of endoglucanase I (Trichoderma resei) in solution

  • P. P. Abuja
  • M. Hayn
  • H. Chen
  • H. Esterbauer
Conference paper
Part of the Progress in Colloid & Polymer Science book series (PROGCOLLOID, volume 93)

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.

Key words

Cellulases endoglucanase small-angle x-ray scattering solution structure 

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Copyright information

© Dr. Dietrich Steinkopff Verlag GmbH & Co. KG 1993

Authors and Affiliations

  • P. P. Abuja
    • 2
  • M. Hayn
    • 1
  • H. Chen
    • 1
  • H. Esterbauer
    • 1
  1. 1.Institut für BiochemieUniversität GrazAustria
  2. 2.Institut für Biophysik und Röntgenstrukturforschung derÖsterreichischen Akademie der WissenschaftenGrazAustria

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