2B7B
Yeast guanine nucleotide exchange factor eEF1Balpha K205A mutant in complex with eEF1A and GDP
Summary for 2B7B
| Entry DOI | 10.2210/pdb2b7b/pdb |
| Related | 1F60 1G7C 1IJE 1IJF 2B7C |
| Descriptor | Elongation factor 1-alpha, elongation factor-1 beta, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | g-protein-gef complex, eef1a, eef1balpha, translation |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Cellular location | Cytoplasm: P02994 |
| Total number of polymer chains | 2 |
| Total formula weight | 60968.55 |
| Authors | Pittman, Y.R.,Valente, L.,Jeppesen, M.G.,Andersen, G.R.,Patel, S.,Kinzy, T.G. (deposition date: 2005-10-04, release date: 2006-05-02, Last modification date: 2023-10-25) |
| Primary citation | Pittman, Y.R.,Valente, L.,Jeppesen, M.G.,Andersen, G.R.,Patel, S.,Kinzy, T.G. Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha J.Biol.Chem., 281:19457-19468, 2006 Cited by PubMed Abstract: To sustain efficient translation, eukaryotic elongation factor B alpha (eEF1B alpha) functions as the guanine nucleotide exchange factor for eEF1A. Stopped-flow kinetics using 2'-(or 3')-O-N-methylanthraniloyl (mant)-GDP showed spontaneous release of nucleotide from eEF1A is extremely slow and accelerated 700-fold by eEF1B alpha. The eEF1B alpha-stimulated reaction was inhibited by Mg2+ with a K(1/2) of 3.8 mM. Previous structural studies predicted the Lys-205 residue of eEF1B alpha plays an important role in promoting nucleotide exchange by disrupting the Mg2+ binding site. Co-crystal structures of the lethal K205A mutant in the catalytic C terminus of eEF1B alpha with eEF1A and eEF1A.GDP established that the lethality was not due to a structural defect. Instead, the K205A mutant drastically reduced the nucleotide exchange activity even at very low concentrations of Mg2+. A K205R eEF1B alpha mutant on the other hand was functional in vivo and showed nearly wild-type nucleotide dissociation rates but almost no sensitivity to Mg2+. These results indicate the significant role of Mg2+ in the nucleotide exchange reaction by eEF1B alpha and establish the catalytic function of Lys-205 in displacing Mg2+ from its binding site. PubMed: 16675455DOI: 10.1074/jbc.M601076200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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