1nel: Difference between revisions

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OCA

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-[[Image:1nel.gif|left|200px]]<br /><applet load="1nel" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1nel, resolution 2.6&Aring;" />
-'''FLUORIDE INHIBITION OF YEAST ENOLASE: CRYSTAL STRUCTURE OF THE ENOLASE-MG2+-F--PI COMPLEX AT 2.6-ANGSTROMS RESOLUTION'''<br />
-==Overview==
+==FLUORIDE INHIBITION OF YEAST ENOLASE: CRYSTAL STRUCTURE OF THE ENOLASE-MG2+-F--PI COMPLEX AT 2.6-ANGSTROMS RESOLUTION==
-Enolase in the presence of its physiological cofactor Mg2+ is inhibited by, fluoride and phosphate ions in a strongly cooperative manner (Nowak, T, Maurer, P. Biochemistry 20:6901, 1981). The structure of the quaternary, complex yeast enolase-Mg(2+)-F(-)-Pi has been determined by X-ray, diffraction and refined to an R = 16.9% for those data with F/sigma (F) &gt;, or = 3 to 2.6 A resolution with a good geometry of the model. The movable, loops of Pro-35-Ala-45, Val-153-Phe-169, and Asp-255-Asn-266 are in the, closed conformation found previously in the precatalytic substrate-enzyme, complex. Calculations of molecular electrostatic potential show that this, conformation stabilizes binding of negatively charged ligands at the Mg2+, ion more strongly than the open conformation observed in the native, enolase. This closed conformation is complementary to the transition, state, which also has a negatively charged ion, hydroxide, at Mg2+. The, synergism of inhibition by F- and Pi most probably is due to the, requirement of Pi for the closed conformation. It is possible that other, Mg(2+)-dependent enzymes that have OH- ions bound to the metal ion in the, transition state also will be inhibited by fluoride ions.
+<StructureSection load='1nel' size='340' side='right'caption='[[1nel]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1nel]] 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=1NEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NEL 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]] 2.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1nel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nel OCA], [https://pdbe.org/1nel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nel RCSB], [https://www.ebi.ac.uk/pdbsum/1nel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nel ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ENO1_YEAST ENO1_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/ne/1nel_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=1nel ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-NEL 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 MG, PO4 and F as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NEL OCA].
+*[[Enolase 3D structures|Enolase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Fluoride inhibition of yeast enolase: crystal structure of the enolase-Mg(2+)-F(-)-Pi complex at 2.6 A resolution., Lebioda L, Zhang E, Lewinski K, Brewer JM, Proteins. 1993 Jul;16(3):219-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8346189 8346189]
+[[Category: Large Structures]]
-[[Category: Phosphopyruvate hydratase]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Brewer MJ]]
-[[Category: Brewer, M.J.]]
+[[Category: Lebioda L]]
-[[Category: Lebioda, L.]]
+[[Category: Lewinski K]]
-[[Category: Lewinski, K.]]
+[[Category: Zhang E]]
-[[Category: Zhang, E.]]
-[[Category: F]]
-[[Category: MG]]
-[[Category: PO4]]
-[[Category: carbon-oxygen lyase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:11:33 2007''