A crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum in the activated state.
A new crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 18.104.22.168) from Nicotiana tabacum has been obtained at alkaline pH with polyethylene glycol 8000 in the presence of a non-ionic detergent, beta-octyl glucoside. The crystals are grown at room temperature by the hanging-drop vapor diffusion technique from a protein solution containing enzyme complexed with CO2, Mg2+, and the transition state analog 2-C-carboxy-D-arabinitol-1,5-bisphosphate. The crystals belong to the the space group P3(1)21 (or P3(2)21) with the cell parameters a = 204.6 A, and c = 117.4 A (1 A = 0.1 nm). The asymmetric unit contains half (L4S4: L, large subunit, 53,000 Mr; S, small subunit, 15,000 Mr) of a hexadecameric molecule (L8S8, 540,000 Mr). The crystals diffract to at least 2.6 A Bragg spacing and are suitable for X-ray structure determination.
Rubisco-the key regulatory enzyme in photosynthetic carbon assimilation-is activated in vivo by the chloroplast enzyme Rubisco activase (Portis, 1990). Previous studies in which Rubisco antisense DNA mutants of tobacco were used have revealed that under some circumstances Rubisco activase can play a central role in regulating the photosynthetic process (Rodermel et al., 1988; Quick et al., 1991a, 1991b; Stitt et al., 1991).
3D print of protein data set 4RUB and base.
Protein Model: Display
Display size of the model is 12cm.
Display base size for 12cm model.
Protein Model: Miniature
Display size of the model is 7cm.
Miniature size base for 7cm model.