The Crystal Structure of the Glutathione S-Transferase-like Domain of Elongation Factor 1Bγ from Saccharomyces Cerevisiae

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Journal of Biological Chemistry

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The crystal structure of the N-terminal 219 residues (domain 1) of the conserved eukaryotic translation elongation factor 1Bγ (eEF1Bγ), encoded by the TEF3 gene in Saccharomyces cerevisiae, has been determined at 3.0 Å 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 eEF1Bγ has no obvious catalytic residue. However, the second form of eEF1Bγ 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·eEF1Bα·eEF1Bγ]2 complex. A 23-residue sequence in the middle of eEF1Bγ is essential for the stable dimerization of eEF1Bγ and the quaternary structure of the eEF1 complex.


This article was originally published as Jeppesen, M.G., Ortiz, P.A., Shepard, W., Kinzy, T.G., Nyborg, J. and Andersen, G.R. (2003) The crystal structure of the GST-like domain of Elongation Factor 1Bï§ from Saccharomyces cerevisiae, J. Biol. Chem., 278: 47190-47198. PMID: 12972429