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[[Image:1nel.gif|left|200px]]


{{Structure
==FLUORIDE INHIBITION OF YEAST ENOLASE: CRYSTAL STRUCTURE OF THE ENOLASE-MG2+-F--PI COMPLEX AT 2.6-ANGSTROMS RESOLUTION==
|PDB= 1nel |SIZE=350|CAPTION= <scene name='initialview01'>1nel</scene>, resolution 2.6&Aring;
<StructureSection load='1nel' size='340' side='right'caption='[[1nel]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=F:FLUORIDE ION'>F</scene>
<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>
|ACTIVITY= [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]  
</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=  
<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>


'''FLUORIDE INHIBITION OF YEAST ENOLASE: CRYSTAL STRUCTURE OF THE ENOLASE-MG2+-F--PI COMPLEX AT 2.6-ANGSTROMS RESOLUTION'''
==See Also==
 
*[[Enolase 3D structures|Enolase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
1NEL is a [[Single protein]] structure of sequence 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=1NEL OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/8346189 8346189]
[[Category: Phosphopyruvate hydratase]]
[[Category: Saccharomyces cerevisiae]]
[[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://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:55:49 2008''

Latest revision as of 10:55, 14 February 2024

FLUORIDE INHIBITION OF YEAST ENOLASE: CRYSTAL STRUCTURE OF THE ENOLASE-MG2+-F--PI COMPLEX AT 2.6-ANGSTROMS RESOLUTIONFLUORIDE INHIBITION OF YEAST ENOLASE: CRYSTAL STRUCTURE OF THE ENOLASE-MG2+-F--PI COMPLEX AT 2.6-ANGSTROMS RESOLUTION

Structural highlights

1nel is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ENO1_YEAST

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1nel, resolution 2.60Å

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