Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus

EMBO J. 1994 Aug 15;13(16):3669-77.

Abstract

The crystal structure of Thermus thermophilus elongation factor G without guanine nucleotide was determined to 2.85 A. This GTPase has five domains with overall dimensions of 50 x 60 x 118 A. The GTP binding domain has a core common to other GTPases with a unique subdomain which probably functions as an intrinsic nucleotide exchange factor. Domains I and II are homologous to elongation factor Tu and their arrangement, both with and without GDP, is more similar to elongation factor Tu in complex with a GTP analogue than with GDP. Domains III and V show structural similarities to ribosomal proteins. Domain IV protrudes from the main body of the protein and has an extraordinary topology with a left-handed cross-over connection between two parallel beta-strands.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • GTP Phosphohydrolase-Linked Elongation Factors / chemistry*
  • GTP Phosphohydrolase-Linked Elongation Factors / metabolism
  • Guanosine Diphosphate / metabolism
  • Guanosine Triphosphate / metabolism
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Elongation Factor G
  • Peptide Elongation Factors / chemistry*
  • Peptide Elongation Factors / metabolism
  • Protein Conformation
  • RNA-Binding Proteins / chemistry
  • Ribosomal Proteins / chemistry
  • Thermus thermophilus / chemistry
  • Thermus thermophilus / enzymology*

Substances

  • Peptide Elongation Factor G
  • Peptide Elongation Factors
  • RNA-Binding Proteins
  • Ribosomal Proteins
  • Guanosine Diphosphate
  • Guanosine Triphosphate
  • GTP Phosphohydrolase-Linked Elongation Factors

Associated data

  • GENBANK/P33998