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1nhy

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Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.

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Retrieved from "http://52.214.119.220/wiki/index.php/1nhy"

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-[[Image:1nhy.jpg|left|200px]]<br /><applet load="1nhy" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1nhy, resolution 3.0&Aring;" />
-'''Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.'''<br />
-==Overview==
+==Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.==
-The crystal structure of the N-terminal 219 residues (domain 1) of the, conserved eukaryotic translation elongation factor 1Bgamma (eEF1Bgamma), encoded by the TEF3 gene in Saccharomyces cerevisiae, has been determined, at 3.0 A resolution by the single wavelength anomalous dispersion, technique. The structure is overall very similar to the glutathione, S-transferase proteins and contains a pocket with architecture highly, homologous to what is observed in glutathione S-transferase enzymes. The, TEF3-encoded form of eEF1Bgamma has no obvious catalytic residue. However, the second form of eEF1Bgamma encoded by the TEF4 gene contains serine 11, which may act catalytically. Based on the x-ray structure and gel, filtration studies, we suggest that the yeast eEF1 complex is organized as, an [eEF1A.eEF1Balpha.eEF1Bgamma]2 complex. A 23-residue sequence in the, middle of eEF1Bgamma is essential for the stable dimerization of, eEF1Bgamma and the quaternary structure of the eEF1 complex.
+<StructureSection load='1nhy' size='340' side='right'caption='[[1nhy]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1nhy]] is a 1 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=1NHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NHY FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nhy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nhy OCA], [https://pdbe.org/1nhy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nhy RCSB], [https://www.ebi.ac.uk/pdbsum/1nhy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nhy ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/EF1G1_YEAST EF1G1_YEAST] Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components. May be involved in transcriptional regulation of MXR1.<ref>PMID:12824466</ref>
+== 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/nh/1nhy_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=1nhy ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-NHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NHY OCA].
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
+== References ==
-==Reference==
+<references/>
-The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae., Jeppesen MG, Ortiz P, Shepard W, Kinzy TG, Nyborg J, Andersen GR, J Biol Chem. 2003 Nov 21;278(47):47190-8. Epub 2003 Sep 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12972429 12972429]
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Andersen GR]]
-[[Category: Andersen, G.R.]]
+[[Category: Jeppesen MG]]
-[[Category: Jeppesen, M.G.]]
+[[Category: Kinzy TG]]
-[[Category: Kinzy, T.G.]]
+[[Category: Nyborg J]]
-[[Category: Nyborg, J.]]
+[[Category: Ortiz P]]
-[[Category: Ortiz, P.]]
-[[Category: SO4]]
-[[Category: gst-like]]
-[[Category: protein synthesis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:16:29 2007''

1nhy

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Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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