Structural and functional domains of cellobiohydrolase I from trichoderma reesei |
| |
Authors: | P. M. Abuja M. Schmuck I. Pilz P. Tomme M. Claeyssens H. Esterbauer |
| |
Affiliation: | (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 |
| |
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 |
| |
Keywords: | Cellobiohydrolase I core CBH I small angle X-ray scattering model for solution structure functional-structural domains |
本文献已被 SpringerLink 等数据库收录! |
|