Supplementary Figure 5: Structural comparison EF-G and D IV loops in solution and on the ribosome.

(a) The overall structure alignment of EF-G in the GTP (PDB 2OM7) and GDP (PDB 2WRI) conformations on the ribosome. When D IVs are aligned and zoomed-in with 90° turn, the tip of loop I moved 10 Å towards P-site upon GTP hydrolysis, whereas loop II remained unchanged. (b) The same proteins of a but in solution. GTP conformer (PDB 1WDT), GDP conformer (PDB 1FNM). The upper tip of D V moved 25 Å. When D IVs were aligned and zoomed-in, the tip of loop I moved 8 Å in the opposite direction compared to its conformation on the ribosome. (c) Structural comparison of EF-G on POST complexes. ecEF-G and ttEF-G are extracted from E. coli and T. thermuphilus POST–EF-G complex (PDB 4KIY and 4KBV), respectively. The overall structures of the two EF-Gs were aligned or D IVs were aligned and zoomed-in with 90° turn. (d) The interface of EF-G with the DC in EF-G–POST (PDB 2WRI). Common domains of EF-G contact only the ribosome whereas D IV interacts directly with tRNA₂–mRNA through its tip region. (e) The zoom-in view of the interface between D IV tip with P-tRNA–mRNA or with DC. A-tRNA (yellow) has been extracted from EF-Tu–PRE (PDB 2Y0U).