Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism

Ilana Agmon, Maya Amit, Tamar Auerbach, Anat Bashan, David Baram, Heike Bartels, Rita Berisio, Inbal Greenberg, Joerg Harms, Harly A.S. Hansen, Maggie Kessler, Erez Pyetan, Frank Schluenzen, Assa Sittner, Ada Yonath, Raz Zarivach

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

Abstract

The linkage between internal ribosomal symmetry and transfer RNA (tRNA) positioning confirmed positional catalysis of amino-acid polymerization. Peptide bonds are formed concurrently with tRNA-3end rotatory motion, in conjunction with the overall messenger RNA (mRNA)/tRNA translocation. Accurate substrate alignment, mandatory for the processivity of protein biosynthesis, is governed by remote interactions. Inherent flexibility of a conserved nucleotide, anchoring the rotatory motion, facilitates chirality discrimination and antibiotics synergism. Potential tRNA interactions explain the universality of the tRNA CCA-end and P-site preference of initial tRNA. The interactions of protein L2 tail with the symmetry-related region periphery explain its conservation and its contributions to nascent chain elongation.

Original languageEnglish
Pages (from-to)20-26
Number of pages7
JournalFEBS Letters
Volume567
Issue number1
DOIs
StatePublished - 1 Jun 2004
Externally publishedYes

Keywords

  • Antibiotics synergism
  • Azithromycin
  • Dual binding
  • Peptide-bond formation
  • Positional catalysis
  • Ribosome
  • Synercid

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