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1e9i

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[[Image:1e9i.jpg|left|200px]]
 
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{{Structure
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==Enolase from E.coli==
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|PDB= 1e9i |SIZE=350|CAPTION= <scene name='initialview01'>1e9i</scene>, resolution 2.48&Aring;
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<StructureSection load='1e9i' size='340' side='right'caption='[[1e9i]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1e9i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E9I FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.48&#8491;</td></tr>
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|GENE= ENO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9i OCA], [https://pdbe.org/1e9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e9i RCSB], [https://www.ebi.ac.uk/pdbsum/1e9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e9i ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9i OCA], [http://www.ebi.ac.uk/pdbsum/1e9i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e9i RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/ENO_ECOLI ENO_ECOLI] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation.<ref>PMID:8610017</ref> <ref>PMID:14981237</ref> <ref>PMID:15522087</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e9/1e9i_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1e9i ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of Escherichia coli enolase (EC 4.2.1.11, phosphopyruvate hydratase), which is a component of the RNA degradosome, has been determined at 2.5 A. There are four molecules in the asymmetric unit of the C2 cell, and in one of the molecules, flexible loops close onto the active site. This closure mimics the conformation of the substrate-bound intermediate. A comparison of the structure of the E. coli enolase with the eukaryotic enolase structures available (lobster and yeast) indicates a high degree of conservation of the hydrophobic core and the subunit interface of this homodimeric enzyme. The dimer interface is enriched in charged residues compared with other protein homodimers, which may explain our observations from analytical ultracentrifugation that dimerisation is affected by ionic strength. The putative role of enolase in the RNA degradosome is discussed; although it was not possible to ascribe a specific role to it, a structural role is possible.
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'''ENOLASE FROM E.COLI'''
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Crystal structure of the Escherichia coli RNA degradosome component enolase.,Kuhnel K, Luisi BF J Mol Biol. 2001 Oct 26;313(3):583-92. PMID:11676541<ref>PMID:11676541</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1e9i" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The crystal structure of Escherichia coli enolase (EC 4.2.1.11, phosphopyruvate hydratase), which is a component of the RNA degradosome, has been determined at 2.5 A. There are four molecules in the asymmetric unit of the C2 cell, and in one of the molecules, flexible loops close onto the active site. This closure mimics the conformation of the substrate-bound intermediate. A comparison of the structure of the E. coli enolase with the eukaryotic enolase structures available (lobster and yeast) indicates a high degree of conservation of the hydrophobic core and the subunit interface of this homodimeric enzyme. The dimer interface is enriched in charged residues compared with other protein homodimers, which may explain our observations from analytical ultracentrifugation that dimerisation is affected by ionic strength. The putative role of enolase in the RNA degradosome is discussed; although it was not possible to ascribe a specific role to it, a structural role is possible.
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*[[Enolase 3D structures|Enolase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1E9I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9I OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Crystal structure of the Escherichia coli RNA degradosome component enolase., Kuhnel K, Luisi BF, J Mol Biol. 2001 Oct 26;313(3):583-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11676541 11676541]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Phosphopyruvate hydratase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Carpousis AJ]]
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[[Category: Carpousis, A J.]]
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[[Category: Kuhnel K]]
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[[Category: Kuhnel, K.]]
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[[Category: Luisi B]]
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[[Category: Luisi, B.]]
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[[Category: degradosome]]
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[[Category: lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:58:01 2008''
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Current revision

Enolase from E.coli

PDB ID 1e9i

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