Response to Comment on “The Mechanism for Activation of GTP Hydrolysis on the Ribosome”

By R. Voorhees, T. Schmeing, A. Kelley, V. Ramakrishnan. Science, 2011

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Molecular architecture of a eukaryotic translational initiation complex (2013, background): “This interaction aligns the SRL with the GTP-binding site on the G-domain in a conformation similar to what has been seen for the activated form of EF-Tu (21).”
Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes (2016, background): “In our complexes, this insertion forms an amphipathic a helix (a2; Figures 6A–6C) connected by a short loop to a helical turn before adopting the same conformation observed in the EF-Tu,GMPPCP complex (Voorhees et al., 2010) (Figure 6A).”
Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation (2020, background): “cerevisiae numbering) toward the catalytic histidine, which is in its “active” configuration, inserted through the hydrophobic gate (25).”
eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining (2014, background): “…Met. ª 2014 The Authors The EMBO Journal Vol 33 | No 10 | 2014 Ribosome-induced GTP hydrolysis by eIF5B Crystal structures of EF-G GDPCP and EF-Tu GDPCP on the ribosome suggest a common mechanism of GTPase activation for both elongation factors (Tourigny et al, 2013; Voorhees et al, 2010).”