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2b7c

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[[Image:2b7c.gif|left|200px]]
[[Image:2b7c.gif|left|200px]]
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{{Structure
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|PDB= 2b7c |SIZE=350|CAPTION= <scene name='initialview01'>2b7c</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_2b7c", creates the "Structure Box" on the page.
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|GENE= TEF5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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{{STRUCTURE_2b7c| PDB=2b7c | SCENE= }}
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|RELATEDENTRY=[[1f60|1F60]], [[1ije|1IJE]], [[1ijf|1IJF]], [[1g7c|1G7C]], [[1b64|1B64]], [[2b7b|2B7B]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b7c OCA], [http://www.ebi.ac.uk/pdbsum/2b7c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b7c RCSB]</span>
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'''Yeast guanine nucleotide exchange factor eEF1Balpha K205A mutant in complex with eEF1A'''
'''Yeast guanine nucleotide exchange factor eEF1Balpha K205A mutant in complex with eEF1A'''
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[[Category: Pittman, Y R.]]
[[Category: Pittman, Y R.]]
[[Category: Valente, L.]]
[[Category: Valente, L.]]
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[[Category: eef1a]]
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[[Category: Eef1a]]
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[[Category: eef1balpha]]
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[[Category: Eef1balpha]]
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[[Category: g-protein/gef complex]]
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[[Category: G-protein/gef complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:56:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:02:24 2008''
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Revision as of 16:56, 3 May 2008

Template:STRUCTURE 2b7c

Yeast guanine nucleotide exchange factor eEF1Balpha K205A mutant in complex with eEF1A


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

2B7C 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 Page seeded by OCA on Sat May 3 19:56:43 2008

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