2al1

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(New page: 200px<br /><applet load="2al1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2al1, resolution 1.50&Aring;" /> '''Crystal Structure An...)
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[[Image:2al1.gif|left|200px]]<br /><applet load="2al1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2al1, resolution 1.50&Aring;" />
 
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'''Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0'''<br />
 
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==Overview==
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==Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0==
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Enolase is a dimeric enzyme that catalyzes the interconversion of, 2-phospho-D-glycerate and phosphoenolpyruvate. This reversible dehydration, is effected by general acid-base catalysis that involves, principally, Lys345 and Glu211 (numbering system of enolase 1 from yeast). The crystal, structure of the inactive E211Q enolase shows that the protein is properly, folded. However, K345 variants have, thus far, failed to crystallize. This, problem was solved by crystallization of an engineered heterodimer of, enolase. The heterodimer was composed of an inactive subunit that has a, K345A mutation and an active subunit that has N80D and N126D surface, mutations to facilitate ion-exchange chromatographic separation of the, three dimeric species. The structure of this heterodimeric variant, in, complex with substrate/product, was obtained at 1.85 A resolution. The, structure was compared to a new structure of wild-type enolase obtained, from crystals belonging to the same space group. Asymmetric dimers having, one subunit exhibiting two of the three active site loops in an open, conformation and the other in a conformation having all three loops closed, appear in both structures. The K345A subunit of the heterodimer is in the, loop-closed conformation; its Calpha carbon atoms closely match those of, the corresponding subunit of wild-type enolase (root-mean-squared, deviation of 0.23 A). The kcat and kcat/Km values of the heterodimer are, approximately half those of the N80D/N126D homodimer, which suggests that, the subunits in solution are kinetically independent. A comparison of, enolase structures obtained from crystals belonging to different space, groups suggests that asymmetric dimers can be a consequence of the, asymmetric positioning of the subunits within the crystal lattice.
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<StructureSection load='2al1' size='340' side='right'caption='[[2al1]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2al1]] is a 2 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=2AL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AL1 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]] 1.5&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</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=2al1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2al1 OCA], [https://pdbe.org/2al1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2al1 RCSB], [https://www.ebi.ac.uk/pdbsum/2al1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2al1 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/al/2al1_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=2al1 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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2AL1 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, CL, K, PEP 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=2AL1 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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Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit., Sims PA, Menefee AL, Larsen TM, Mansoorabadi SO, Reed GH, J Mol Biol. 2006 Jan 20;355(3):422-31. Epub 2005 Nov 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16309698 16309698]
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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: Larsen TM]]
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[[Category: Larsen, T.M.]]
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[[Category: Mansoorabadi SO]]
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[[Category: Mansoorabadi, S.O.]]
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[[Category: Menefee AL]]
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[[Category: Menefee, A.L.]]
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[[Category: Reed GH]]
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[[Category: Reed, G.H.]]
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[[Category: Sims PA]]
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[[Category: Sims, P.A.]]
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[[Category: 2PG]]
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[[Category: CL]]
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[[Category: K]]
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[[Category: MG]]
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[[Category: PEP]]
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[[Category: beta barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:11:51 2007''
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Current revision

Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0

PDB ID 2al1

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