1NHY

Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.

Summary for 1NHY

• Entry DOI: 10.2210/pdb1nhy/pdb
• Related: 1FW1 3LJR
• Descriptor: Elongation factor 1-gamma 1, SULFATE ION (2 entities in total)
• Functional Keywords: protein synthesis, gst-like, translation
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P29547
• Total number of polymer chains: 1
• Total formula weight: 25046.11

Authors

Jeppesen, M.G.,Ortiz, P.,Kinzy, T.G.,Andersen, G.R.,Nyborg, J. (deposition date: 2002-12-20, release date: 2003-01-14, Last modification date: 2024-11-13)

Primary citation

Jeppesen, M.G.,Ortiz, P.,Shepard, W.,Kinzy, T.G.,Nyborg, J.,Andersen, G.R.
The Crystal Structure of the Glutathione S-Transferase-like Domain of Elongation Factor 1B{gamma} from Saccharomyces cerevisiae.
J.Biol.Chem., 278:47190-47198, 2003

PubMed Abstract: 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.

PubMed: 12972429
DOI: 10.1074/jbc.M306630200

Experimental method

X-RAY DIFFRACTION (3 Å)