2b7b: Difference between revisions

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New page: left|200px<br /><applet load="2b7b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b7b, resolution 2.6Å" /> '''Yeast guanine nucleot...
 
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[[Image:2b7b.gif|left|200px]]<br /><applet load="2b7b" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2b7b.gif|left|200px]]<br /><applet load="2b7b" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2b7b, resolution 2.6&Aring;" />
caption="2b7b, resolution 2.6&Aring;" />
'''Yeast guanine nucleotide exchange factor eEF1Balpha K205A mutant in complex with eEF1A and GDP'''<br />
'''Yeast guanine nucleotide exchange factor eEF1Balpha K205A mutant in complex with eEF1A and GDP'''<br />


==Overview==
==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.
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==
==About this Structure==
2B7B is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with GDP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B7B OCA].  
2B7B is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B7B OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Andersen, G.R.]]
[[Category: Andersen, G R.]]
[[Category: Jeppesen, M.G.]]
[[Category: Jeppesen, M G.]]
[[Category: Kinzy, T.G.]]
[[Category: Kinzy, T G.]]
[[Category: Patel, S.]]
[[Category: Patel, S.]]
[[Category: Pittman, Y.R.]]
[[Category: Pittman, Y R.]]
[[Category: Valente, L.]]
[[Category: Valente, L.]]
[[Category: GDP]]
[[Category: GDP]]
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[[Category: g-protein/gef complex]]
[[Category: g-protein/gef complex]]


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