7N2U
Elongating 70S ribosome complex in a hybrid-H1 pre-translocation (PRE-H1) conformation
This is a non-PDB format compatible entry.
Summary for 7N2U
| Entry DOI | 10.2210/pdb7n2u/pdb |
| EMDB information | 24133 |
| Descriptor | 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (61 entities in total) |
| Functional Keywords | elongation complex, trna, mrna, pre-translocation, ribosome |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 56 |
| Total formula weight | 2219366.32 |
| Authors | Rundlet, E.J.,Holm, M.,Schacherl, M.,Natchiar, K.S.,Altman, R.B.,Spahn, C.M.T.,Myasnikov, A.G.,Blanchard, S.C. (deposition date: 2021-05-29, release date: 2021-07-14, Last modification date: 2021-08-11) |
| Primary citation | Rundlet, E.J.,Holm, M.,Schacherl, M.,Natchiar, S.K.,Altman, R.B.,Spahn, C.M.T.,Myasnikov, A.G.,Blanchard, S.C. Structural basis of early translocation events on the ribosome. Nature, 595:741-745, 2021 Cited by PubMed Abstract: Peptide-chain elongation during protein synthesis entails sequential aminoacyl-tRNA selection and translocation reactions that proceed rapidly (2-20 per second) and with a low error rate (around 10 to 10 at each step) over thousands of cycles. The cadence and fidelity of ribosome transit through mRNA templates in discrete codon increments is a paradigm for movement in biological systems that must hold for diverse mRNA and tRNA substrates across domains of life. Here we use single-molecule fluorescence methods to guide the capture of structures of early translocation events on the bacterial ribosome. Our findings reveal that the bacterial GTPase elongation factor G specifically engages spontaneously achieved ribosome conformations while in an active, GTP-bound conformation to unlock and initiate peptidyl-tRNA translocation. These findings suggest that processes intrinsic to the pre-translocation ribosome complex can regulate the rate of protein synthesis, and that energy expenditure is used later in the translocation mechanism than previously proposed. PubMed: 34234344DOI: 10.1038/s41586-021-03713-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.53 Å) |
Structure validation
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