Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression

Anat Bashan, Ilana Agmon, Raz Zarivach, Frank Schluenzen, Joerg Harms, Rita Berisio, Heike Bartels, Francois Franceschi, Tamar Auerbach, Harly A.S. Hansen, Elizaveta Kossoy, Maggie Kessler, Ada Yonath

Research output: Contribution to journalArticlepeer-review

247 Scopus citations

Abstract

Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3′ end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism.

Original languageEnglish
Pages (from-to)91-102
Number of pages12
JournalMolecular Cell
Volume11
Issue number1
DOIs
StatePublished - 1 Jan 2003
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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