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. 2016 Oct 31;7:13314. doi: 10.1038/ncomms13314

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Copyright © 2016, The Author(s)

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(a) EF-Tu, in the form of ternary complex (EF-Tu̇GTṖaa-tRNA), binds the ribosome at the opening of the accommodation corridor²⁰,²¹,²²,²³,²⁴,²⁶,²⁹. (b) When EF-Tu is restrained to its GTP conformation on the ribosome, and a minimal affinity for aa-tRNA is included, the barrier to elbow accommodation is reduced by ∼10 k_BT (red curve), relative to the barrier when EF-Tu is absent (black curve). (c,d) Two-dimensional free-energy profiles, calculated for the models that lack EF-Tu (c) and include EF-Tu (d). There is a drastic reduction in the range of accessible conformations of aa-tRNA when EF-Tu is bound to the ribosome. This leads to destabilization, and shift in position, of the A/T-like ensemble (A/T^−Tu in c and A/T^+Tu in d).