2b7b
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= TEF5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= TEF5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1f60|1F60]], [[1ije|1IJE]], [[1ijf|1IJF]], [[1g7c|1G7C]], [[2b7c|2B7C]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b7b OCA], [http://www.ebi.ac.uk/pdbsum/2b7b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b7b RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Pittman, Y R.]] | [[Category: Pittman, Y R.]] | ||
[[Category: Valente, L.]] | [[Category: Valente, L.]] | ||
| - | [[Category: GDP]] | ||
[[Category: eef1a]] | [[Category: eef1a]] | ||
[[Category: eef1balpha]] | [[Category: eef1balpha]] | ||
[[Category: g-protein/gef complex]] | [[Category: g-protein/gef complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:02:23 2008'' |
Revision as of 23:02, 30 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | TEF5 (Saccharomyces cerevisiae) | ||||||
| Related: | 1F60, 1IJE, 1IJF, 1G7C, 2B7C
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Yeast guanine nucleotide exchange factor eEF1Balpha K205A mutant in complex with eEF1A and GDP
Overview
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.
About this Structure
2B7B is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha., Pittman YR, Valente L, Jeppesen MG, Andersen GR, Patel S, Kinzy TG, J Biol Chem. 2006 Jul 14;281(28):19457-68. Epub 2006 May 4. PMID:16675455
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