Ilana Agmon, 1. Department of Structural Biology, The Weizmann Institute, 76100 Rehovot, Israel
1 Anat Bashan, 2. Department of Structural Biology, The Weizmann Institute, 76100 Rehovot, Israel
2 Raz Zarivach, 3. Department of Structural Biology, The Weizmann Institute, 76100 Rehovot, Israel
3 Ada Yonath4. Department of Structural Biology, The Weizmann Institute, 76100 Rehovot, Israel
4 Abstract
The sizable symmetrical region, comprising 180 ribosomal RNA nucleotides, which has been identified in and around the peptidyl transferase center (PTC) in crystal structures of eubacterial and archaeal large ribosomal subunits, indicates its universality, confirms that the ribosome is a ribozyme and evokes the suggestion that the PTC evolved by gene fusion. The symmetrical region can act as a center that coordinates amino acid polymerization by transferring intra-ribosomal signals between remote functional locations, as it connects, directly or through its extensions, the PTC, the three tRNA sites, the tunnel entrance, and the regions hosting elongation factors. Significant deviations from the overall symmetry stabilize the entire region and can be correlated with the shaping and guiding of the motion of the tRNA 3′-end from the A- into the P-site. The linkage between the elaborate PTC architecture and the spatial arrangements of the tRNA 3′-ends revealed the rotatory mechanism that integrates peptide bond formation, translocation within the PTC and nascent protein entrance into the exit tunnel. The positional catalysis exerted by the ribosome places the reactants in stereochemistry close to the intermediate state and facilitates the catalytic contribution of the P-site tRNA 2′-hydroxyl.
