Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site

J Mol Biol. 2000 Nov 3;303(4):593-603. doi: 10.1006/jmbi.2000.4168.


The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 A. The mutant has a more closed structure than that previously reported for wild-type EF-G. This is obtained by a 10 degrees rigid rotation of domains III, IV and V with regard to domains I and II. This rotation results in a displacement of the tip of domain IV by approximately 9 A. The structure of domain III is now fully visible and reveals the double split beta-alpha-beta motif also observed for EF-G domain V and for several ribosomal proteins. A large number of fusidic acid resistant mutations found in domain III have now been possible to locate. Possible locations for the effector loop and a possible binding site for fusidic acid are discussed in relation to some of the fusidic acid resistant mutations.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Amino Acid Substitution / genetics*
  • Binding Sites
  • Conserved Sequence
  • Crystallography, X-Ray
  • Drug Resistance, Microbial
  • Fusidic Acid / metabolism
  • Guanosine Diphosphate / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Elongation Factor G / chemistry*
  • Peptide Elongation Factor G / genetics
  • Peptide Elongation Factor G / metabolism*
  • Point Mutation / genetics*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Thermus thermophilus / chemistry*
  • Thermus thermophilus / genetics


  • Peptide Elongation Factor G
  • Guanosine Diphosphate
  • Fusidic Acid

Associated data

  • PDB/1FNM