2b7b: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2b7b.gif|left|200px]]


{{Structure
==Yeast guanine nucleotide exchange factor eEF1Balpha K205A mutant in complex with eEF1A and GDP==
|PDB= 2b7b |SIZE=350|CAPTION= <scene name='initialview01'>2b7b</scene>, resolution 2.6&Aring;
<StructureSection load='2b7b' size='340' side='right'caption='[[2b7b]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>
<table><tr><td colspan='2'>[[2b7b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B7B FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
|GENE= TEF5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b7b OCA], [https://pdbe.org/2b7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b7b RCSB], [https://www.ebi.ac.uk/pdbsum/2b7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b7b ProSAT]</span></td></tr>
|RELATEDENTRY=[[1f60|1F60]], [[1ije|1IJE]], [[1ijf|1IJF]], [[1g7c|1G7C]], [[2b7c|2B7C]]
</table>
|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>
== Function ==
}}
[https://www.uniprot.org/uniprot/EF1A_YEAST EF1A_YEAST]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b7/2b7b_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b7b ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''Yeast guanine nucleotide exchange factor eEF1Balpha K205A mutant in complex with eEF1A and GDP'''
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<ref>PMID:16675455</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2b7b" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 
== References ==
==About this Structure==
<references/>
2B7B is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B7B OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Andersen, G R.]]
[[Category: Andersen GR]]
[[Category: Jeppesen, M G.]]
[[Category: Jeppesen MG]]
[[Category: Kinzy, T G.]]
[[Category: Kinzy TG]]
[[Category: Patel, S.]]
[[Category: Patel S]]
[[Category: Pittman, Y R.]]
[[Category: Pittman YR]]
[[Category: Valente, L.]]
[[Category: Valente L]]
[[Category: eef1a]]
[[Category: eef1balpha]]
[[Category: g-protein/gef complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:02:23 2008''
Retrieved from "https://proteopedia.org/2b7b"