ArticleRNA (New York, N.Y.)2017
Induced fit of the peptidyl-transferase center of the ribosome and conformational freedom of the esterified amino acids.
Article in RNA (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Co-Translational Incorporation ofJournal of the American Chemical Society · 2026Article
- Context-dependent translation inhibition as a cancer therapeutic modality.Nature communications · 2026Article
- Ribosome selectivity and nascent chain context in modulating the incorporation of fluorescent non-canonical amino acid into proteins.Scientific reports · 2022Article
- Genetic code degeneracy is established by the decoding center of the ribosome.Nucleic acids research · 2022Article
- The Peptidyl Transferase Center: a Window to the Past.Microbiology and molecular biology reviews : MMBR · 2021Article
- Peptidyl transferase center decompaction and structural constraints during early protein elongation on the ribosome.Scientific reports · 2021Article
- The Ancient History of Peptidyl Transferase Center Formation as Told by Conservation and Information Analyses.Life (Basel, Switzerland) · 2020Article
- RQT complex dissociates ribosomes collided on endogenous RQC substrate SDD1.Nature structural & molecular biology · 2020Article
- Article
- Nervous-Like Circuits in the Ribosome Facts, Hypotheses and Perspectives.International journal of molecular sciences · 2019Review
- Mechanistic insights into the slow peptide bond formation with D-amino acids in the ribosomal active site.Nucleic acids research · 2019Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The catalytic site of most enzymes can efficiently handle only one substrate. In contrast, the ribosome is capable of polymerizing at a similar rate at least 20 different kinds of amino acids from aminoacyl-tRNA carriers while using just one catalytic site, the peptidyl-transferase center (PTC). An induced-fit mechanism has been uncovered in the PTC, but a possible connection between this mechanism and the uniform handling of the substrates has not been investigated. We present an analysis of published ribosome structures supporting the hypothesis that the induced fit eliminates unreactive rotamers predominantly populated for some A-site aminoacyl esters before induction. We show that this hypothesis is fully consistent with the wealth of kinetic data obtained with these substrates. Our analysis reveals that induction constrains the amino acids into a reactive conformation in a side-chain independent manner. It allows us to highlight the rationale of the PTC structural organization, which confers to the ribosome the very unusual ability to handle large as well as small substrates.
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