Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural snapshots of actively translating human ribosomes.
Journal, issue, pages	Cell, Vol. 161, Issue 4, Page 845-857, Year 2015
Publish date	May 7, 2015
Authors	Elmar Behrmann / Justus Loerke / Tatyana V Budkevich / Kaori Yamamoto / Andrea Schmidt / Pawel A Penczek / Matthijn R Vos / Jörg Bürger / Thorsten Mielke / Patrick Scheerer / Christian M T Spahn /
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 ...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.
External links	Cell / PubMed:25957688 / PubMed Central
Methods	EM (single particle)
Resolution	3.5 - 9.5 Å
Structure data	2875 5aj0 EMDB-2875, PDB-5aj0: Cryo electron microscopy of actively translating human polysomes (POST state). Method: EM (single particle) / Resolution: 3.5 Å EMDB-2902: Cryo electron microscopy of actively translating human polysomes (POST-i2 state). Method: EM (single particle) / Resolution: 7.4 Å EMDB-2903: Cryo electron microscopy of actively translating human polysomes (POST-i3 state). Method: EM (single particle) / Resolution: 6.7 Å EMDB-2904: Cryo electron microscopy of actively translating human polysomes (rotated-1 PRE state). Method: EM (single particle) / Resolution: 7.3 Å EMDB-2905: Cryo electron microscopy of actively translating human polysomes (rotated-2 PRE state). Method: EM (single particle) / Resolution: 5.4 Å EMDB-2906: Cryo electron microscopy of actively translating human polysomes (PRE* state). Method: EM (single particle) / Resolution: 9.5 Å EMDB-2907: Cryo electron microscopy of actively translating human polysomes (classical iPRE state). Method: EM (single particle) / Resolution: 9.2 Å EMDB-2908: Cryo electron microscopy of actively translating human polysomes (decoding/post-hydrolysis state). Method: EM (single particle) / Resolution: 7.1 Å EMDB-2909: Cryo electron microscopy of actively translating human polysomes (classical-1 PRE state). Method: EM (single particle) / Resolution: 7.1 Å EMDB-2910: Cryo electron microscopy of actively translating human polysomes (pre-recycling state). Method: EM (single particle) / Resolution: 8.0 Å EMDB-2911: Cryo electron microscopy of actively translating human polysomes (decoding/post-dissociation state). Method: EM (single particle) / Resolution: 6.5 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-ZN: Unknown entry
Source	homo sapiens (human) yersinia pseudotuberculosis (bacteria)
Keywords	RIBOSOME / MAMMALIAN RIBOSOME / TRANSLATION / POLYSOME / CRYO ELECTRON MICROSCOPY / ELONGATION CYCLE