| Autor: |
Wilhelm, P., Abuja, P., Meisenberger, O., Pilz, I., Bowien, B., Pal, G., Hahn, U., Saenger, W. |
| Zdroj: |
European Biophysics Journal; 1986, Vol. 14 Issue 2, p93-96, 4p |
| Abstrakt: |
The quaternary structure of ribulose-1,5-bisphosphate carboxylase-oxygenase (rubisco) from Rhodospirillum rubrum, an enzyme consisting of two large subunits, L, was investigated by small-angle X-ray scattering. In the presence of HCOand Mg, rubisco is in the active state and displays a radius of gyration of 2.96 nm, a maximum diameter of 9.5 nm and a volume of 170 nm. A model is presented where the subunits are arranged back-to-back, rotated relative to each other by 90°, and shifted by 1.3 nm. Upon inactivation by removal of HCOand Mg, the model swells slightly without any distinct changes in configuration. This contrasts with our previous observations with rubisco from Alcaligenes eutrophus, an enzyme composed of small (S) and large (L) subunits, LS, where inactivation gives rise to substantial changes in configuration. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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