A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases

@article{Wang2012ACP,
  title={A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases},
  author={Li Wang and Fang Yang and Dejiu Zhang and Zhi Chen and Rui-Ming Xu and Knud H. Nierhaus and Weimin Gong and Yan Qin},
  journal={Nature Structural \&Molecular Biology},
  year={2012},
  volume={19},
  pages={403-410}
}
When elongation factor G (EF-G) binds to the ribosome, it first makes contact with the C-terminal domain (CTD) of L12 before interacting with the N-terminal domain (NTD) of L11. Here we have identified a universally conserved residue, Pro22 of L11, that functions as a proline switch (PS22), as well as the corresponding center of peptidyl-prolyl cis-trans isomerase (PPIase) activity on EF-G that drives the cis-trans isomerization of PS22. Only the cis configuration of PS22 allows direct contact… Expand
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