Small angle x-ray study on the structure of active and inactive ribulose bisphosphate carboxylase from Alcaligenes eutrophus. Evidence for a configurational change.
Two small angle x-ray scattering curves have been obtained from active and inactive ribulose 1,5-bisphosphate carboxylase from Alcaligenes eutrophus. The radius of gyration was calculated to be R = 47.8 +/- 0.1 nm for the active enzyme and R = 49.2 +/- 0.1 nm for the inactive enzyme. The maximum particle dimension amounts to 13.5 +/- 0.5 nm for the active and 15.7 +/- 0.5 nm for the inactive enzyme. A model of the active carboxylase is presented. It is in good agreement with models derived from electron microscopical data. Model calculations for the inactive enzyme show some evidence for a configurational change.
D000421:Alcaligenes / Q000201:enzymology*; D011487:Protein Conformation; D012273:Ribulose-Bisphosphate Carboxylase; D014961:X-Ray Diffraction
D012273:Ribulose-Bisphosphate Carboxylase