The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae.
The crystal structure of the N-terminal 219 residues (domain 1) of the conserved eukaryotic translation elongation factor 1Bgamma (eEF1Bgamma), encoded by the TEF3 gene in Saccharomyces cerevisiae, has been determined at 3.0 A resolution by the single wavelength anomalous dispersion technique. The structure is overall very similar to the glutathione S-transferase proteins and contains a pocket with architecture highly homologous to what is observed in glutathione S-transferase enzymes. The TEF3-encoded form of eEF1Bgamma has no obvious catalytic residue. However, the second form of eEF1Bgamma encoded by the TEF4 gene contains serine 11, which may act catalytically. Based on the x-ray structure and gel filtration studies, we suggest that the yeast eEF1 complex is organized as an [eEF1A.eEF1Balpha.eEF1Bgamma]2 complex. A 23-residue sequence in the middle of eEF1Bgamma is essential for the stable dimerization of eEF1Bgamma and the quaternary structure of the eEF1 complex.
Jeppesen
Mads Gravers
MG
Department of Molecular Biology, University of Arhus, Gustav Wieds vej 10 C, 8000 Arhus C, Denmark.
Ortiz
Pedro
P
Shepard
William
W
Kinzy
Terri Goss
TG
Nyborg
Jens
J
Andersen
Gregers Rom
GR
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D019281:Dimerization; D005982:Glutathione Transferase / Q000737:chemistry; D015394:Molecular Structure; D020648:Peptide Elongation Factor 1 / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*
D020648:Peptide Elongation Factor 1; D029701:Saccharomyces cerevisiae Proteins; D005982:Glutathione Transferase