Abstract
Comparison of the crystal structures of the L2 and L8S8 forms of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum and spinach respectively, reveals a remarkable similarity in the overall architecture of the L2 building blocks in the two enzymes. Within the L subunits, no large conformational differences such as domain-domain rotations were found. In spite of a somewhat different packing of the L subunits in the L2 dimer, the active sites of the two enzymes are highly conserved. Significant local conformational differences are, however, observed for the C-terminal part of the polypeptide chains as well as for loop 7, helix alpha 7, loop 8 and helix alpha 8 in the barrel domain. The small subunit forms extensive interactions with one of these alpha helices, alpha 8, in the spinach L8S8 enzyme. The loops are at the active site and one of them forms a phosphate binding site for the substrate. We suggest that the small subunit modulates substrate binding and, possibly, the carboxylation/oxygenation ratio by inducing conformational changes in the active site through interactions distant from this site.
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