7N1P

Elongating 70S ribosome complex in a classical pre-translocation (PRE-C) conformation

This is a non-PDB format compatible entry.

Summary for 7N1P

• Entry DOI: 10.2210/pdb7n1p/pdb
• EMDB information: 24120
• Descriptor: 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (64 entities in total)
• Functional Keywords: elongation complex, trna, mrna, ribosome
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 58
• Total formula weight: 2255982.44

Authors

Rundlet, E.J.,Holm, M.,Schacherl, M.,Natchiar, S.K.,Altman, R.B.,Spahn, C.M.T.,Myasnikov, A.G.,Blanchard, S.C. (deposition date: 2021-05-28, 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

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: 34234344
DOI: 10.1038/s41586-021-03713-x

Experimental method

ELECTRON MICROSCOPY (2.33 Å)