Crystal structure of apo-glycolate oxidase.
The crystal structure of the apoform of the alpha/beta-barrel enzyme glycolate oxidase has been determined to 2.6 A resolution. Removal of the tightly bound cofactor FMN has a very strong influence on the protein structure; it is converted into a very flexible state, verging on a molten globule type of structure. The asymmetric unit contains two subunits with different conformations to each other and to the holo-enzyme. The secondary structures are preserved, but their mutual arrangement has changed to some extent introducing cavities into the protein. The largest structural shifts are, however, found in the loops.
Sandalova
T
T
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
Lindqvist
Y
Y
D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D008958:Models, Molecular; D010944:Plants / Q000201:enzymology; D011487:Protein Conformation; D014961:X-Ray Diffraction
D000429:Alcohol Oxidoreductases; C020821:glycollate oxidase