Cross-crystal averaging reveals that the structure of the peptidyl-transferase center is the same in the 70S ribosome and the 50S subunit.

Abstract

Recently, two crystal structures of the Thermus thermophilus 70S ribosome in the same functional state were determined at 2.8 and 3.7 A resolution but were different throughout. The most functionally significant structural differences are in the conformation of the peptidyl-transferase center (PTC) and the interface between the PTC and the CCA end of the P-site tRNA. Likewise, the 3.7 A PTC differed from the functionally equivalent structure of the Haloarcula marismortui 50S subunit. To ascertain whether the 3.7 A model does indeed differ from the other two, we performed cross-crystal averaging of the two 70S data sets. The unbiased maps suggest that the conformation of the PTC-CCA in the two 70S crystal forms is identical to that of the 2.8 A 70S model as well as that of the H. marismortui 50S subunit. We conclude that the structure of the PTC is the same in the functionally equivalent 70S ribosome and the 50S subunit.