5AJ0
Cryo electron microscopy of actively translating human polysomes (POST state).
This is a non-PDB format compatible entry.
Summary for 5AJ0
| Entry DOI | 10.2210/pdb5aj0/pdb |
| EMDB information | 2875 |
| Descriptor | 5.8S ribosomal RNA, 60S ribosomal protein L9, 60S ribosomal protein L10, ... (87 entities in total) |
| Functional Keywords | ribosome, mammalian ribosome, translation, polysome, cryo electron microscopy, elongation cycle |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 86 |
| Total formula weight | 3924116.05 |
| Authors | Behrmann, E.,Loerke, J.,Budkevich, T.V.,Yamamoto, K.,Schmidt, A.,Penczek, P.A.,Vos, M.R.,Burger, J.,Mielke, T.,Scheerer, P.,Spahn, C.M.T. (deposition date: 2015-02-19, release date: 2015-05-20, Last modification date: 2019-12-18) |
| Primary citation | Behrmann, E.,Loerke, J.,Budkevich, T.V.,Yamamoto, K.,Schmidt, A.,Penczek, P.A.,Vos, M.R.,Burger, J.,Mielke, T.,Scheerer, P.,Spahn, C.M.T. Structural Snapshots of Actively Translating Human Ribosomes Cell(Cambridge,Mass.), 161:845-857, 2015 Cited by PubMed Abstract: 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. PubMed: 25957688DOI: 10.1016/j.cell.2015.03.052 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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