Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A

J Mol Biol. 1987 Jun 5;195(3):555-79. doi: 10.1016/0022-2836(87)90183-5.


The structure of a C-terminal fragment of the ribosomal protein L7/L12 from Escherichia coli has been refined using crystallographic data to 1.7 A resolution. The R-value is 17.4%. Six residues at the N terminus are too disordered in the structure to be localized. These residues are probably part of a hinge in the complete L7/L12 molecule. The possibility that a 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A patch of invariant residues on the surface of the dimer is probably involved in functional interactions with elongation factors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • Crystallography
  • Escherichia coli / analysis
  • Hydrogen Bonding
  • Models, Molecular
  • Protein Conformation
  • Ribosomal Proteins*


  • Bacterial Proteins
  • Ribosomal Proteins
  • ribosomal protein L7-L12