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. 2022 Oct 3;5:1052. doi: 10.1038/s42003-022-04019-y

Fig. 3. EF-Ts exhibits a diverse binding conformation among different species.

Fig. 3

a Superimposition of EF-Tu•EF-Ts complex structures among Mtb (marine, PDB: 7VMX), E. coli (light pink, PDB: 1EFU), and T. thermophilus (green, PDB: 1AIP). The RMSD values between Mtb and E. coli or T. thermophilus were 1.214 Å or 1.309 Å, respectively. b Superimposition of EF-Tu structures among Mtb, E. coli, and T. thermophilus. c Superimposition of EF-Ts structures among Mtb, E. coli, and T. thermophilus. The numbers denoted significant differences among the three structures. d The detailed difference of EF-Ts structures among three species, according to (c). ‘1’, the extra helix of E. coli EF-Ts for binding with EF-Tu Domain I. ‘2’ and ‘4’, the helices in the T. thermophilus EF-Ts, absent in Mtb and E. coli, which were not involved in binding with EF-Tu. ‘3’, the α10 and α11 helices that shifted about 4.7 Å or 6.0 Å within three species, respectively.