2b7b: Difference between revisions
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|PDB= 2b7b |SIZE=350|CAPTION= <scene name='initialview01'>2b7b</scene>, resolution 2.6Å | |PDB= 2b7b |SIZE=350|CAPTION= <scene name='initialview01'>2b7b</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5 | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> | ||
|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]) | ||
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[[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 Sun Mar 23 14:42:45 2008'' | ||
Revision as of 15:42, 23 March 2008
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| , resolution 2.6Å | |||||||
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| Gene: | TEF5 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Yeast guanine nucleotide exchange factor eEF1Balpha K205A mutant in complex with eEF1A and GDP
OverviewOverview
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 StructureAbout this Structure
2B7B is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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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