Structural transitions during activation and ligand binding in hexadecameric Rubisco inferred from the crystal structure of the activated unliganded spinach enzyme.

Activation of ribulose-1,5-bisphosphate carboxylase oxygenase (Rubisco; EC 4.1.1.39) by CO2 involves carbamylation of Lys 201 and the subsequent binding of a magnesium ion to complete the active site. The refined crystal structure of activated Rubisco shows that the magnesium ligands are Asp 203, Glu 204, the carbamate of Lys 201, and three water molecules. Structural differences between the unactivated and activated forms are minimal. Substrate binding replaces water ligands around the metal and triggers substantial structural changes in loops covering the active site. This leads to a contraction and tightening of the structure of the large subunits with the movements transmitted to and modulated by the small subunits.