6GC7
50S ribosomal subunit assembly intermediate state 1
Summary for 6GC7
Entry DOI | 10.2210/pdb6gc7/pdb |
EMDB information | 4378 4379 4380 4381 4382 |
Descriptor | 23S ribosomal RNA, 50S ribosomal protein L21, 50S ribosomal protein L22, ... (17 entities in total) |
Functional Keywords | assembly precursor 48s 50s biogenesis in vitro reconstitution, ribosome |
Biological source | Escherichia coli K-12 More |
Total number of polymer chains | 17 |
Total formula weight | 1141442.99 |
Authors | Nikolay, R.,Hilal, T.,Qin, B.,Loerke, J.,Buerger, J.,Mielke, T.,Spahn, C.M.T. (deposition date: 2018-04-17, release date: 2018-06-20, Last modification date: 2024-05-15) |
Primary citation | Nikolay, R.,Hilal, T.,Qin, B.,Mielke, T.,Burger, J.,Loerke, J.,Textoris-Taube, K.,Nierhaus, K.H.,Spahn, C.M.T. Structural Visualization of the Formation and Activation of the 50S Ribosomal Subunit during In Vitro Reconstitution. Mol. Cell, 70:881-893.e3, 2018 Cited by PubMed Abstract: The assembly of ribosomal subunits is an essential prerequisite for protein biosynthesis in all domains of life. Although biochemical and biophysical approaches have advanced our understanding of ribosome assembly, our mechanistic comprehension of this process is still limited. Here, we perform an in vitro reconstitution of the Escherichia coli 50S ribosomal subunit. Late reconstitution products were subjected to high-resolution cryo-electron microscopy and multiparticle refinement analysis to reconstruct five distinct precursors of the 50S subunit with 4.3-3.8 Å resolution. These assembly intermediates define a progressive maturation pathway culminating in a late assembly particle, whose structure is more than 96% identical to a mature 50S subunit. Our structures monitor the formation and stabilization of structural elements in a nascent particle in unprecedented detail and identify the maturation of the rRNA-based peptidyl transferase center as the final critical step along the 50S assembly pathway. PubMed: 29883607DOI: 10.1016/j.molcel.2018.05.003 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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