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. Author manuscript; available in PMC: 2021 Jul 6.
Published in final edited form as: J Mol Biol. 2020 Feb 13;432(9):3064–3077. doi: 10.1016/j.jmb.2020.01.038

Figure 4. Conformations of EF-Tu during aa-tRNA accommodation.

Figure 4.

(A) The classical closed conformation of EF-Tu bound to GDPNP (PDB ID: 1EFT) with a DI-DII distance of 18Å, DI-DIII distance of 30Å, and a switch I-DIII distance of 32Å. (B) The intermediate conformation of EF-Tu resolved by structure based simulations where the DI-DII and DI-DIII distances have increased to 28 and 41 Å, respectively and switch one is in an intermediate proximity to DIII at a distance of 20Å. (C) The classical open conformation of EF-Tu bound to GDP (PDB 1EFC). DI-DII is fully open at a distance of 40Å, DI has approached DIII and switch I is packing with DIII.