Ribosomal proteins and elongation factors

Curr Opin Struct Biol. 1995 Dec;5(6):721-7. doi: 10.1016/0959-440x(95)80003-4.

Abstract

Structural work on the translation machinery has recently undergone rapid progress. It is now known that six out of nine ribosomal proteins have an RNA-binding fold, and two domains of elongation factors Tu and G have very similar folds. In addition, the complex of EF-Tu with a GTP analogue and Phe-tRNA(Phe) has a structure that overlaps exceedingly well with that of EF-G-GDP. These findings obviously have functional implications.

Publication types

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

MeSH terms

  • Fungal Proteins*
  • Guanosine Diphosphate / metabolism
  • Models, Molecular
  • Peptide Elongation Factor G
  • Peptide Elongation Factor Tu / chemistry
  • Peptide Elongation Factor Tu / metabolism
  • Peptide Elongation Factors / chemistry*
  • Peptide Elongation Factors / metabolism
  • Protein Biosynthesis
  • Protein Conformation
  • RNA, Ribosomal / chemistry
  • Ribosomal Proteins / chemistry*
  • Ribosomal Proteins / metabolism
  • Ribosomes / chemistry
  • Ribosomes / ultrastructure
  • Saccharomyces cerevisiae Proteins

Substances

  • Fungal Proteins
  • Peptide Elongation Factor G
  • Peptide Elongation Factors
  • RNA, Ribosomal
  • Ribosomal Proteins
  • Saccharomyces cerevisiae Proteins
  • YEF3 protein, S cerevisiae
  • Guanosine Diphosphate
  • Peptide Elongation Factor Tu