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2ezu

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[[Image:2ezu.png|left|200px]]
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==Pyruvate oxidase variant F479W in complex with reaction intermediate 2-acetyl-thiamin diphosphate==
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<StructureSection load='2ezu' size='340' side='right' caption='[[2ezu]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ezu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactobacillus_plantarum Lactobacillus plantarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EZU FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HTL:2-ACETYL-THIAMINE+DIPHOSPHATE'>HTL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pow|1pow]], [[1pox|1pox]], [[1y9d|1y9d]], [[2ez4|2ez4]], [[2ez8|2ez8]], [[2ez9|2ez9]], [[2ezt|2ezt]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pox5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1590 Lactobacillus plantarum])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_oxidase Pyruvate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.3.3 1.2.3.3] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ezu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ezu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ezu RCSB], [http://www.ebi.ac.uk/pdbsum/2ezu PDBsum]</span></td></tr>
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<table>
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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/ez/2ezu_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/chain_selection.php?pdb_ID=2ata 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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Enzymes that use the cofactor thiamin diphosphate (ThDP, 1), the biologically active form of vitamin B(1), are involved in numerous metabolic pathways in all organisms. Although a theory of the cofactor's underlying reaction mechanism has been established over the last five decades, the three-dimensional structures of most major reaction intermediates of ThDP enzymes have remained elusive. Here, we report the X-ray structures of key intermediates in the oxidative decarboxylation of pyruvate, a central reaction in carbon metabolism catalyzed by the ThDP- and flavin-dependent enzyme pyruvate oxidase (POX)3 from Lactobacillus plantarum. The structures of 2-lactyl-ThDP (LThDP, 2) and its stable phosphonate analog, of 2-hydroxyethyl-ThDP (HEThDP, 3) enamine and of 2-acetyl-ThDP (AcThDP, 4; all shown bound to the enzyme's active site) provide profound insights into the chemical mechanisms and the stereochemical course of thiamin catalysis. These snapshots also suggest a mechanism for a phosphate-linked acyl transfer coupled to electron transfer in a radical reaction of pyruvate oxidase.
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{{STRUCTURE_2ezu| PDB=2ezu | SCENE= }}
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The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography.,Wille G, Meyer D, Steinmetz A, Hinze E, Golbik R, Tittmann K Nat Chem Biol. 2006 Jun;2(6):324-8. Epub 2006 May 7. PMID:16680160<ref>PMID:16680160</ref>
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===Pyruvate oxidase variant F479W in complex with reaction intermediate 2-acetyl-thiamin diphosphate===
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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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{{ABSTRACT_PUBMED_16680160}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2ezu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactobacillus_plantarum Lactobacillus plantarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZU OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:016680160</ref><references group="xtra"/>
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[[Category: Lactobacillus plantarum]]
[[Category: Lactobacillus plantarum]]
[[Category: Pyruvate oxidase]]
[[Category: Pyruvate oxidase]]

Revision as of 23:44, 29 September 2014

Pyruvate oxidase variant F479W in complex with reaction intermediate 2-acetyl-thiamin diphosphate

2ezu, resolution 2.16Å

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