Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
Abuja, PM; Pilz, I; Claeyssens, M; Tomme, P.
Domain structure of cellobiohydrolase II as studied by small angle X-ray scattering: close resemblance to cellobiohydrolase I.
Biochem Biophys Res Commun. 1988; 156(1):180-185
Doi: 10.1016/S0006-291X(88)80821-0
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- Führende Autor*innen der Med Uni Graz
- Abuja Peter Michael
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- Abstract:
- Evidence for a domain structure of cellobiohydrolase II (CBH II, 58 kDa) from Trichoderma reesei (Teeri et al., 1987; Tomme et al., 1988) is corroborated by results from SAXS experiments. They indicate a 'tadpole' structure for the intact CBH II in solution (Dmax = 21.5 +/- 0.5 nm; Rg = 5.4 +/- 0.1 nm) and a more isotropic, ellipsoid shape for the core protein (Dmax = 6.0 +/- 0.3 nm; Rg = 2.1 +/- 0.1 nm). The latter was obtained by partial proteolysis with papain which cleaves the native CBH II to give two fragments (Tomme et al., 1988): the core (45 kDa) with the active (hydrolytic) domain and a smaller fragment (11 kDa) coinciding with the tail part of the model and containing the binding domain for unsoluble cellulose. This peptide fragment is conserved in most cellulolytic enzymes from Trichoderma reesei (Teeri et al., 1987). It contains a conserved region (block A) and glycosylated parts (blocks B and B' duplicated and located N-terminally in CBH II). In spite of different domain arrangements in CBH I (blocks B-A at C-terminals) SAXS measurements (Abuja et al., 1988) indicate similar tertiary structures for both cellobiohydrolases although discrete differences in the tail parts exist.
- Find related publications in this database (using NLM MeSH Indexing)
- Binding Sites -
- Cellulose 1,4-beta-Cellobiosidase -
- Glycoside Hydrolases - metabolism
- Isoenzymes - metabolism
- Models, Molecular - metabolism
- Protein Conformation - metabolism
- Trichoderma - enzymology
- X-Ray Diffraction - enzymology