2b7b: Difference between revisions

Revision as of 14:45, 28 July 2008

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File:2b7b.png

Template:STRUCTURE 2b7b

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

Template:ABSTRACT PUBMED 16675455

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

Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha., Andersen GR, Pedersen L, Valente L, Chatterjee I, Kinzy TG, Kjeldgaard M, Nyborg J, Mol Cell. 2000 Nov;6(5):1261-6. PMID:11106763

Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex., Andersen GR, Valente L, Pedersen L, Kinzy TG, Nyborg J, Nat Struct Biol. 2001 Jun;8(6):531-4. PMID:11373622

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 {{STRUCTURE_2b7b|  PDB=2b7b  |  SCENE=  }}
-'''Yeast guanine nucleotide exchange factor eEF1Balpha K205A mutant in complex with eEF1A and GDP'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16675455}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16675455 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16675455}}
 ==About this Structure==
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 ==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:[http://www.ncbi.nlm.nih.gov/pubmed/16675455 16675455]
+Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha., Andersen GR, Pedersen L, Valente L, Chatterjee I, Kinzy TG, Kjeldgaard M, Nyborg J, Mol Cell. 2000 Nov;6(5):1261-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11106763 11106763]
+Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex., Andersen GR, Valente L, Pedersen L, Kinzy TG, Nyborg J, Nat Struct Biol. 2001 Jun;8(6):531-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11373622 11373622]
 [[Category: Protein complex]]
 [[Category: Saccharomyces cerevisiae]]
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 [[Category: Eef1balpha]]
 [[Category: G-protein/gef complex]]
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