4V6D
Crystal structure of the E. coli 70S ribosome in an intermediate state of ratcheting
This is a non-PDB format compatible entry.
Summary for 4V6D
Entry DOI | 10.2210/pdb4v6d/pdb |
Related | 3I1M 3I1N 3I1O 3I1P 3I1Z 3I20 3I21 3I22 |
Descriptor | 30S ribosomal protein S2, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (59 entities in total) |
Functional Keywords | ribosome structure, protein-rna complex, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, antibiotic resistance, repressor, transcription, transcription regulation, transcription termination, translation regulation, trna-binding, methylation, endonuclease, hydrolase, nuclease, ribosome |
Biological source | Escherichia coli K-12 More |
Total number of polymer chains | 108 |
Total formula weight | 4308870.17 |
Authors | Zhang, W.,Dunkle, J.A.,Cate, J.H.D. (deposition date: 2009-06-27, release date: 2014-07-09, Last modification date: 2024-10-30) |
Primary citation | Zhang, W.,Dunkle, J.A.,Cate, J.H. Structures of the ribosome in intermediate States of ratcheting. Science, 325:1014-1017, 2009 Cited by PubMed Abstract: Protein biosynthesis on the ribosome requires repeated cycles of ratcheting, which couples rotation of the two ribosomal subunits with respect to each other, and swiveling of the head domain of the small subunit. However, the molecular basis for how the two ribosomal subunits rearrange contacts with each other during ratcheting while remaining stably associated is not known. Here, we describe x-ray crystal structures of the intact Escherichia coli ribosome, either in the apo-form (3.5 angstrom resolution) or with one (4.0 angstrom resolution) or two (4.0 angstrom resolution) anticodon stem-loop tRNA mimics bound, that reveal intermediate states of intersubunit rotation. In the structures, the interface between the small and large ribosomal subunits rearranges in discrete steps along the ratcheting pathway. Positioning of the head domain of the small subunit is controlled by interactions with the large subunit and with the tRNA bound in the peptidyl-tRNA site. The intermediates observed here provide insight into how tRNAs move into the hybrid state of binding that precedes the final steps of mRNA and tRNA translocation. PubMed: 19696352DOI: 10.1126/science.1175275 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.814 Å) |
Structure validation
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