Structural changes in cellobiohydrolase I upon binding of a macromolecular ligand as evident by SAXS investigations.
Xylan from Rhodymenia palmata binds to the cellobiohydrolase I from Trichoderma reesei (CBH I) or its core protein, inhibiting their activity. Adsorption onto microcrystalline cellulose (Avicel) is reduced approximately 30% for intact CBH I and nearly 50% for the core, whereas the effects with cellobiose are negligible. Structural changes concomitant with this binding are studied in solution by small angle X-ray scattering. In the "tadpole" structure typical for the CBH I [Abuja et al., 1988] the lengthening of the tail part is the most salient observation when xylan is present which accounts for an increase in Dmax (18.0 to 22.0 nm) and radius of gyration (4.74 to 5.18 nm). When xylan binds to the core the radius of gyration remains nearly unchanged. Here a model can be constructed showing a xylan molecule on the surface of the core protein near the tail part.
Abuja
P M
PM
Institut für Physikalische Chemie, Universität Graz, Austria.
Pilz
I
I
Tomme
P
P
Claeyssens
M
M
D000327:Adsorption; D002482:Cellulose; D043366:Cellulose 1,4-beta-Cellobiosidase; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D008961:Models, Structural; D011134:Polysaccharides / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D014242:Trichoderma / Q000201:enzymology; D014961:X-Ray Diffraction; D014990:Xylans / Q000378:metabolism* / Q000494:pharmacology
D008024:Ligands; D011134:Polysaccharides; D014990:Xylans; D002482:Cellulose; D006026:Glycoside Hydrolases; D043366:Cellulose 1,4-beta-Cellobiosidase