4.5 Article

Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome

Journal

NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 16, Issue 5, Pages 528-533

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1577

Keywords

-

Funding

  1. Medical Research Council UK
  2. Wellcome Trust
  3. Agouron Institute
  4. Louis-Jeantet Foundation
  5. Gates-Cambridge scholarship
  6. MRC [MC_U105184332] Funding Source: UKRI
  7. Medical Research Council [MC_U105184332] Funding Source: researchfish

Ask authors/readers for more resources

Protein synthesis is catalyzed in the peptidyl transferase center (PTC), located in the large (50S) subunit of the ribosome. No high-resolution structure of the intact ribosome has contained a complete active site including both A- and P-site tRNAs. In addition, although past structures of the 50S subunit have found no ordered proteins at the PTC, biochemical evidence suggests that specific proteins are capable of interacting with the 3' ends of tRNA ligands. Here we present structures, at 3.6-angstrom and 3.5-angstrom resolution respectively, of the 70S ribosome in complex with A- and P-site tRNAs that mimic pre- and post-peptidyl-transfer states. These structures demonstrate that the PTC is very similar between the 50S subunit and the intact ribosome. They also reveal interactions between the ribosomal proteins L16 and L27 and the tRNA substrates, helping to elucidate the role of these proteins in peptidyl transfer.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available