7enl

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(New page: 200px<br /><applet load="7enl" size="450" color="white" frame="true" align="right" spinBox="true" caption="7enl, resolution 2.2&Aring;" /> '''MECHANISM OF ENOLASE:...)
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[[Image:7enl.gif|left|200px]]<br /><applet load="7enl" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="7enl, resolution 2.2&Aring;" />
 
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'''MECHANISM OF ENOLASE: THE CRYSTAL STRUCTURE OF ENOLASE-MG2+-PHOSPHOGLYCERATE(SLASH) PHOSPHOENOLPYRUVATE COMPLEX AT 2.2-ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==MECHANISM OF ENOLASE: THE CRYSTAL STRUCTURE OF ENOLASE-MG2+-PHOSPHOGLYCERATE(SLASH) PHOSPHOENOLPYRUVATE COMPLEX AT 2.2-ANGSTROMS RESOLUTION==
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Enolase in the presence of Mg2+ catalyzes the elimination of H2O from, 2-phosphoglyceric acid (PGA) to form phosphoenolpyruvate (PEP) and the, reverse reaction, the hydration of PEP to PGA. The structure of the, ternary complex yeast enolase-Mg2(+)-PGA/PEP has been determined by X-ray, diffraction and refined by crystallographic restrained least-squares to an, R = 16.9% for those data with I/sigma (I) greater than or equal to 2 to, 2.2-A resolution with a good geometry of the model. The structure, indicates the substrate molecule in the active site has its hydroxyl group, coordinated to the Mg2+ ion. The carboxylic group interacts with the side, chains of His373 and Lys396. The phosphate group is H-bonded to the, guanidinium group of Arg374. A water molecule H-bonded to the carboxylic, groups of Glu168 and Glu211 is located at a 2.6-A distance from carbon-2, of the substrate in the direction of its proton. We propose that this, cluster functions as the base abstracting the proton in the catalytic, process. The proton is probably transferred, first to the water molecule, then to Glu168, and further to the substrate hydroxyl to form a water, molecule. Some analogy is apparent between the initial stages of the, enolase reverse reaction, the hydration of PEP, and the proteolytic, mechanism of the metallohydrolases carboxypeptidase A and thermolysin. The, substrate/product binding is accompanied by large movements of loops, Ser36-His43 and Ser158-Gly162. The role of these conformational changes is, not clear at this time.
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<StructureSection load='7enl' size='340' side='right'caption='[[7enl]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7enl]] 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=7ENL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ENL FirstGlance]. <br>
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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]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PG:2-PHOSPHOGLYCERIC+ACID'>2PG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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=7enl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7enl OCA], [https://pdbe.org/7enl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7enl RCSB], [https://www.ebi.ac.uk/pdbsum/7enl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7enl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ENO1_YEAST ENO1_YEAST]
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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/en/7enl_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=7enl ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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7ENL 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 and 2PG 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=7ENL OCA].
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*[[Enolase 3D structures|Enolase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Mechanism of enolase: the crystal structure of enolase-Mg2(+)-2-phosphoglycerate/phosphoenolpyruvate complex at 2.2-A resolution., Lebioda L, Stec B, Biochemistry. 1991 Mar 19;30(11):2817-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2007120 2007120]
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[[Category: Large Structures]]
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[[Category: Phosphopyruvate hydratase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Lebioda L]]
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[[Category: Lebioda, L.]]
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[[Category: Stec B]]
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[[Category: Stec, B.]]
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[[Category: 2PG]]
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[[Category: MG]]
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[[Category: carbon-oxygen lyase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:20:39 2007''
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Current revision

MECHANISM OF ENOLASE: THE CRYSTAL STRUCTURE OF ENOLASE-MG2+-PHOSPHOGLYCERATE(SLASH) PHOSPHOENOLPYRUVATE COMPLEX AT 2.2-ANGSTROMS RESOLUTION

PDB ID 7enl

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