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6enl

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(New page: 200px<br /><applet load="6enl" size="450" color="white" frame="true" align="right" spinBox="true" caption="6enl, resolution 2.2&Aring;" /> '''INHIBITION OF ENOLASE...)
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[[Image:6enl.gif|left|200px]]<br /><applet load="6enl" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="6enl, resolution 2.2&Aring;" />
 
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'''INHIBITION OF ENOLASE: THE CRYSTAL STRUCTURES OF ENOLASE-CA2+-PHOSPHOGLYCERATE AND ENOLASE-ZN2+-PHOSPHOGLYCOLATE COMPLEXES AT 2.2-ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==INHIBITION OF ENOLASE: THE CRYSTAL STRUCTURES OF ENOLASE-CA2+-PHOSPHOGLYCERATE AND ENOLASE-ZN2+-PHOSPHOGLYCOLATE COMPLEXES AT 2.2-ANGSTROMS RESOLUTION==
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Enolase is a metalloenzyme which catalyzes the elimination of H2O from, 2-phosphoglyceric acid (PGA) to form phosphoenolpyruvate (PEP). Mg2+ and, Zn2+ are cofactors which strongly bind and activate the enzyme. Ca2+ also, binds strongly but does not produce activity. Phosphoglycolate (PG) is a, competitive inhibitor of enolase. The structures of two inhibitory ternary, complexes: yeast enolase-Ca2(+)-PGA and yeast enolase-Zn2(+)-PG, were, determined by X-ray diffraction to 2.2-A resolution and were refined by, crystallographic least-squares to R = 14.8% and 15.7%, respectively, with, good geometries of the models. These structures are compared with the, structure of the precatalytic ternary complex enolase-Mg2(+)-PGA/PEP, (Lebioda &amp; Stec, 1991). In the complex enolase-Ca2(+)-PGA, the PGA, molecule coordinates to the Ca2+ ion with the hydroxyl group, as in the, precatalytic complex. The conformation of the PGA molecule is however, different. In the active complex, the organic part of the PGA molecule is, planar, similar to the product. In the inhibitory complex, the carboxylic, group is in an orthonormal conformation. In the inhibitory complex, enolase-Zn2(+)-PG, the PG molecule coordinates with the carboxylic group, in a monodentate mode. In both inhibitory complexes, the conformational, changes in flexible loops, which were observed in the precatalytic, complex, do not take place. The lack of catalytic metal ion binding, suggests that these conformational changes are necessary for the formation, of the catalytic metal ion binding site.
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<StructureSection load='6enl' size='340' side='right'caption='[[6enl]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6enl]] 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=6ENL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ENL 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=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6enl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6enl OCA], [https://pdbe.org/6enl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6enl RCSB], [https://www.ebi.ac.uk/pdbsum/6enl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6enl 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/6enl_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=6enl 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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6ENL 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 PGA and ZN 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=6ENL 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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Inhibition of enolase: the crystal structures of enolase-Ca2(+)- 2-phosphoglycerate and enolase-Zn2(+)-phosphoglycolate complexes at 2.2-A resolution., Lebioda L, Stec B, Brewer JM, Tykarska E, Biochemistry. 1991 Mar 19;30(11):2823-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2007121 2007121]
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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: PGA]]
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[[Category: ZN]]
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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 15:31:59 2007''
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Current revision

INHIBITION OF ENOLASE: THE CRYSTAL STRUCTURES OF ENOLASE-CA2+-PHOSPHOGLYCERATE AND ENOLASE-ZN2+-PHOSPHOGLYCOLATE COMPLEXES AT 2.2-ANGSTROMS RESOLUTION

PDB ID 6enl

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