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  Structural Snapshots of Actively Translating Human Ribosomes

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-A738-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-A739-1
Genre: Journal Article

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 Creators:
Behrmann, E.1, Author              
Loerke, J.2, Author
Budkevich, T. V.2, Author
Yamamoto, K.2, Author
Schmidt, A.2, Author
Penczek, P. A.3, Author
Vos, M. R.4, Author
Bürger, J.5, Author              
Mielke, T.5, Author              
Scheerer, P.2, Author
Spahn, C. M. T.2, Author
Affiliations:
1Research Group Structural Dynamics of Proteins, Center of Advanced European Studies and Research (caesar), Max Planck Society, ou_2173687              
2Institut für Medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany, ou_persistent22              
3Department of Biochemistry and Molecular Biology, The University of Texas Medical School, 6431 Fannin MSB 6.220, Houston, TX 77054, USA, ou_persistent22              
4FEI Company, Nanoport Europe, Achtseweg Noord 5, 5651 GG Eindhoven, the Netherlands, ou_persistent22              
5Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

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 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.

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Language(s): eng - English
 Dates: 2015-05-07
 Publication Status: Published in print
 Pages: -
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 Identifiers: DOI: 10.1016/j.cell.2015.03.052
ISSN: 0092-8674
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Title: Cell
  Alternative Title : Cell
Source Genre: Journal
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Publ. Info: Elsevier
Pages: - Volume / Issue: 161 (4) Sequence Number: - Start / End Page: 845 - 857 Identifier: -