English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Structural Snapshots of Actively Translating Human Ribosomes

MPS-Authors
/persons/resource/persons118827

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

/persons/resource/persons73855

Bürger,  J.
Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society;

/persons/resource/persons50431

Mielke,  T.
Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society;

Locator
There are no locators available
Fulltext (public)

Behrmann.pdf
(Publisher version), 7MB

Supplementary Material (public)
There is no public supplementary material available
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-0000-0029-A738-3
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.