High resolution structure of the large ribosomal subunit from a mesophilic eubacterium

Cell. 2001 Nov 30;107(5):679-88. doi: 10.1016/s0092-8674(01)00546-3.


We describe the high resolution structure of the large ribosomal subunit from Deinococcus radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and functionally relevant ligands. The over-all structure of D50S is similar to that from the archae bacterium Haloarcula marismortui (H50S); however, a detailed comparison revealed significant differences, for example, in the orientation of nucleotides in peptidyl transferase center and in the structures of many ribosomal proteins. Analysis of ribosomal features involved in dynamic aspects of protein biosynthesis that are partially or fully disordered in H50S revealed the conformations of intersubunit bridges in unbound subunits, suggesting how they may change upon subunit association and how movements of the L1-stalk may facilitate the exit of tRNA.

MeSH terms

  • Bacterial Proteins / chemistry
  • Crystallography, X-Ray
  • Gram-Positive Cocci / chemistry*
  • Gram-Positive Cocci / ultrastructure
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Structure
  • Nucleic Acid Conformation
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • RNA, Bacterial / chemistry
  • RNA, Bacterial / metabolism
  • RNA, Ribosomal / chemistry*
  • RNA, Transfer / chemistry
  • RNA, Transfer / metabolism
  • Ribosomal Proteins / chemistry*
  • Ribosomes / chemistry*
  • Ribosomes / ultrastructure


  • Bacterial Proteins
  • Macromolecular Substances
  • RNA, Bacterial
  • RNA, Ribosomal
  • Ribosomal Proteins
  • RNA, Transfer

Associated data

  • PDB/1KC9