Skip to main content
. Author manuscript; available in PMC: 2010 Mar 5.
Published in final edited form as: Q Rev Biophys. 2009 Aug;42(3):159–200. doi: 10.1017/S0033583509990060

Fig. 18.

Fig. 18

Conformational changes in ADPR-eEF2 as a direct result of GTP hydrolysis. (a) Density attributed to ADPR-eEF2 from the 80S•ADPR-eEF2•GDPNP map (red) is virtually superimposable with that from the 80S•ADPR-eEF2•GDPNP•sordarin map (gray), a map equivalent to the 80S•ADPR-eEF2•GDPNP shown in Fig. 18b (see Taylor et al. 2007 for details). Conversely, superimposition of density attributed to ADPR-eEF2 from the 80S•ADPR-eEF2•GDP•sordarin map (blue) with that from the 80S•ADPR-eEF2•GDPNP•sordarin map (gray) demonstrates significant conformational changes in the factor that are due exclusively to GTP hydrolysis. (b) The atomic models from the 80S•ADPR-eEF2•GDPNP (red) and 80S•ADPReEF2•GDPNP•sordarin (gray) complexes are very similar, whereas a comparison of the 80S•ADPR-eEF2•GDP•sordarin (blue) and 80S•ADPR-eEF2•GDPNP•sordarin (gray) atomic models shows evidence of rearrangements due to GTP hydrolysis. The arrows indicate the direction and magnitude of the conformational changes of the factor. All atomic models in this figure were obtained by flexible fitting using real-space refinement. Data reproduced from Taylor et al. (2007), copyright (2007) Nature Publishing Group.