Small-angle X-ray scattering studies on cellobiose dehydrogenase from Phanerochaete chrysosporium
| Autor: | Peter Zipper, Gunnar Henriksson, Dieter Lehner, Göran Pettersson |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular Cellobiose dehydrogenase Stereochemistry Protein Conformation Biophysics Flavin group Heme Biochemistry chemistry.chemical_compound Structural Biology Papain Scattering Radiation Molecular Biology biology Small-angle X-ray scattering Chemistry Scattering Basidiomycota X-Rays biology.organism_classification Peptide Fragments Crystallography Flavin-Adenine Dinucleotide Phanerochaete Carbohydrate Dehydrogenases Linker |
| Zdroj: | Biochimica et biophysica acta. 1293(1) |
| ISSN: | 0006-3002 |
| Popis: | Limited proteolysis of cellobiose dehydrogenase (CDH) from the white rot fungus Phanerochaete chrysosporium by papain cleaves the enzyme into two fragments containing flavin (FAD) and heme, respectively. Small-angle X-ray scattering (SAXS) was employed to investigate size and shape of intact CDH and of its fragments in solution. The largest dimension of CDH amounts to about 18 nm, whereas the corresponding quantity of each of the two fragments is only around 9 nm. CDH as well as its fragments appear to be of prolate shape, the cross-section of the FAD fragment (diameter 4.3 to 5.1 nm) being considerably larger than that of the heme fragment (diameter 3.3 nm). These findings suggest a collinear arrangement of the two domains in the CDH particle. Simulations based on the method of finite elements corroborate this structure model and furthermore suggest the existence of a possibly flexible linker between the two domains |
| Databáze: | OpenAIRE |
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