2wva
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2wva is ON HOLD Authors: Pei, X.Y., Erixon, K., Luisi, B.F., Leeper, F.J. Description: Structural insights into the pre-reaction state of pyruvate ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural insights into the pre-reaction state of pyruvate decarboxylase from Zymomonas mobilis== | |
| + | <StructureSection load='2wva' size='340' side='right'caption='[[2wva]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2wva]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WVA FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
| + | <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=PYR:PYRUVIC+ACID'>PYR</scene>, <scene name='pdbligand=TPU:2-{1-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-METHYL-1H-1,2,3-TRIAZOL-4-YL}ETHYL+TRIHYDROGEN+DIPHOSPHATE'>TPU</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=2wva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wva OCA], [https://pdbe.org/2wva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wva RCSB], [https://www.ebi.ac.uk/pdbsum/2wva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wva ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PDC_ZYMMO PDC_ZYMMO] | ||
| + | == 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/wv/2wva_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=2wva ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pyruvate decarboxylase (PDC) uses thiamine diphosphate as an essential cofactor to catalyze the formation of acetaldehyde on the pathway of ethanol synthesis. Here we report the crystallographic image of a prereaction intermediate of a bacterial pyruvate decarboxylase prepared by cocrystallizing the enzyme with pyruvate and a stable analogue of the cofactor's activated ylid form. A second crystal structure of PDC in complex with fluoride shows that the ion organizes a water molecule that occludes the pyruvate binding site, accounting for the inhibitory effect of the halide. Also reported is a structure of the cofactor-free apo form, which when compared to the structure of the holo form indicates how thiamine diphosphate organizes the active site pocket of pyruvate decarboxylase to support catalysis. Guided by the structural and enzymatic data, we propose roles for several key residues in the catalytic mechanism. | ||
| - | + | Structural Insights into the Prereaction State of Pyruvate Decarboxylase from Zymomonas mobilis .,Pei XY, Erixon KM, Luisi BF, Leeper FJ Biochemistry. 2010 Feb 5. PMID:20099870<ref>PMID:20099870</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2wva" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Pyruvate decarboxylase|Pyruvate decarboxylase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Zymomonas mobilis]] | ||
| + | [[Category: Erixon K]] | ||
| + | [[Category: Leeper FJ]] | ||
| + | [[Category: Luisi BF]] | ||
| + | [[Category: Pei XY]] | ||
Current revision
Structural insights into the pre-reaction state of pyruvate decarboxylase from Zymomonas mobilis
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