Protein synthesis at atomic resolution: mechanistics of translation in the light of highly resolved structures for the ribosome

Curr Protein Pept Sci. 2002 Feb;3(1):1-53. doi: 10.2174/1389203023380846.


Our understanding of the process of translation has progressed rapidly since the availability of highly resolved structures for the ribosome. A wealth of information has emerged in terms of both RNA and protein structure and the interplay between them. This has prompted us to revisit the astonishing "treasure trove" of functional data regarding the ribosome that has accumulated over the past decades. Here we try a systematic synopsis of these ribosomal functions in light of the cryo-electron microscopic structures (resolution >7 A) and the atomic x-ray structures (>2.4 A) of the ribosome.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Codon, Terminator / metabolism
  • Models, Biological
  • Nucleic Acid Conformation
  • Peptide Biosynthesis
  • Peptide Elongation Factor G / metabolism
  • Peptide Elongation Factor Tu / metabolism
  • Peptide Initiation Factors / metabolism
  • Peptide Termination Factors / metabolism
  • Peptidyl Transferases / metabolism
  • Protein Biosynthesis / physiology*
  • Protein Conformation
  • RNA, Ribosomal / chemistry
  • RNA, Ribosomal / metabolism
  • RNA, Transfer / chemistry
  • RNA, Transfer / metabolism
  • Ribosomal Proteins / chemistry
  • Ribosomal Proteins / physiology
  • Ribosomes / metabolism
  • Ribosomes / physiology*
  • Ribosomes / ultrastructure


  • Codon, Terminator
  • Peptide Elongation Factor G
  • Peptide Initiation Factors
  • Peptide Termination Factors
  • RNA, Ribosomal
  • Ribosomal Proteins
  • RNA, Transfer
  • Peptidyl Transferases
  • Peptide Elongation Factor Tu