The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution

EMBO J. 1994 Aug 15;13(16):3661-8. doi: 10.1002/j.1460-2075.1994.tb06675.x.


Elongation factor G (EF-G) catalyzes the translocation step of protein synthesis in bacteria, and like the other bacterial elongation factor, EF-Tu--whose structure is already known--it is a member of the GTPase superfamily. We have determined the crystal structure of EF-G--GDP from Thermus thermophilus. It is an elongated molecule whose large, N-terminal domain resembles the G domain of EF-Tu, except for a 90 residue insert, which covers a surface that is involved in nucleotide exchange in EF-Tu and other G proteins. The tertiary structures of the second domains of EF-G and EF-Tu are nearly identical, but the relative placement of the first two domains in EF-G--GDP resembles that seen in EF-Tu--GTP, not EF-Tu--GDP. The remaining three domains of EF-G look like RNA binding domains, and have no counterparts in EF-Tu.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • GTP Phosphohydrolase-Linked Elongation Factors / chemistry*
  • GTP Phosphohydrolase-Linked Elongation Factors / metabolism
  • Guanosine Diphosphate / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Chain Elongation, Translational
  • Peptide Elongation Factor G
  • Peptide Elongation Factor Tu / chemistry
  • Peptide Elongation Factors / chemistry*
  • Peptide Elongation Factors / metabolism
  • Thermus thermophilus / chemistry
  • Thermus thermophilus / enzymology*


  • Peptide Elongation Factor G
  • Peptide Elongation Factors
  • Guanosine Diphosphate
  • GTP Phosphohydrolase-Linked Elongation Factors
  • Peptide Elongation Factor Tu