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Journal Article

Structural Snapshots of Actively Translating Human Ribosomes

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Behrmann,  Elmar
Max Planck Research Group Structural Dynamics of Proteins, Center of Advanced European Studies and Research (caesar), Max Planck Society;

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Citation

Behrmann, E., Loerke, J., Budkevich, T., Yamamoto, K., Schmidt, A., Penczek, P., et al. (2015). Structural Snapshots of Actively Translating Human Ribosomes. Cell, 161(4), 845-857. doi:10.1016/j.cell.2015.03.052.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0028-60AA-3
Abstract
Summary Macromolecular machines, such as the ribosome, undergo large-scale conformational changes during their functional cycles. Although their mode of action is often compared to that of mechanical machines, a crucial difference is that, at the molecular dimension, thermodynamic effects dominate functional cycles, with proteins fluctuating stochastically between functional states defined by energetic minima on an energy landscape. Here, we have used cryo-electron microscopy to image ex-vivo-derived human polysomes as a source of actively translating ribosomes. Multiparticle refinement and 3D variability analysis allowed us to visualize a variety of native translation intermediates. Significantly populated states include not only elongation cycle intermediates in pre- and post-translocational states, but also eEF1A-containing decoding and termination/recycling complexes. Focusing on the post-translocational state, we extended this assessment to the single-residue level, uncovering striking details of ribosome-ligand interactions and identifying both static and functionally important dynamic elements.