Structural and functional domains of cellobiohydrolase I from trichoderma reesei |
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Authors: | P M Abuja M Schmuck I Pilz P Tomme M Claeyssens H Esterbauer |
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Institution: | (1) Institut für Physikalische Chemie, Karl-Franzens Universität Graz, Heinrichstrasse 28, A-8010 Graz, Austria;(2) Laboratorium voor Biochemie, Fakulteit Wetenschappen, Rijksuniversiteit Gent, K. L. Lederganckstraat 35, B-9000 Gent, Belgium;(3) Institut für Biochemie, Karl-Franzens Universität Graz, Halbärthgasse 5, A-8010 Graz, Austria |
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Abstract: | Limited proteolysis (papain) of the cellobiohydrolase I (CBH I, 65 kDa) from Trichoderma reesei led to the seperation of two functional domains: a core protein (55 kDa) containing the active site, and a C-terminal glycopeptide (10 kDa) implicated in binding to the insoluble matrix (cellulose). The quaternary structures of the intact CBH I and its core in solution are now compared by small angle X-ray scattering (SAXS) measurements. The molecular parameters derived for the core (Rg=2.09 nm, Dmax=6.5 nm) and for the intact enzyme (Rg=4.27 nm, Dmax=18 nm) indicate very different shapes. The resulting models show a tadpole -like structure for the intact enzyme where the isotropic part coincides with the core protein and the flexible tail part should be identified with the C-terminal glycopeptide. Thus in this enzyme, functional differentiation is reflected in structural peculiarities.Abbreviations SAXS
small angle X-ray scattering
- SDS-PAGE
SDS-polyacrylamide gel electrophoresis
- IEF-PAG
polyacrylamide gel isoelectric focusing; cellobiohydrolase (CBH, 1,4- -glucan cellobio hydrolase (E.C.3.2.1.91))
- Dmax
maximum diameter
- Rg
radius of gyration |
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Keywords: | Cellobiohydrolase I core CBH I small angle X-ray scattering model for solution structure functional-structural domains |
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