1w88

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[[Image:1w88.png|left|200px]]
 
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{{STRUCTURE_1w88| PDB=1w88 | SCENE= }}
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==The crystal structure of pyruvate dehydrogenase E1(D180N,E183Q) bound to the peripheral subunit binding domain of E2==
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<StructureSection load='1w88' size='340' side='right'caption='[[1w88]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1w88]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W88 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]] 2.3&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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=1w88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w88 OCA], [https://pdbe.org/1w88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w88 RCSB], [https://www.ebi.ac.uk/pdbsum/1w88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w88 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ODPB_GEOSE ODPB_GEOSE] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
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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/w8/1w88_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=1w88 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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Thiamine diphosphate (ThDP) is used as a cofactor in many key metabolic enzymes. We present evidence that the ThDPs in the two active sites of the E1 (EC 1.2.4.1) component of the pyruvate dehydrogenase complex communicate over a distance of 20 angstroms by reversibly shuttling a proton through an acidic tunnel in the protein. This "proton wire" permits the co-factors to serve reciprocally as general acid/base in catalysis and to switch the conformation of crucial active-site peptide loops. This synchronizes the progression of chemical events and can account for the oligomeric organization, conformational asymmetry, and "ping-pong" kinetic properties of E1 and other thiamine-dependent enzymes.
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===THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1(D180N, E183Q) BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2===
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A molecular switch and proton wire synchronize the active sites in thiamine enzymes.,Frank RA, Titman CM, Pratap JV, Luisi BF, Perham RN Science. 2004 Oct 29;306(5697):872-6. PMID:15514159<ref>PMID:15514159</ref>
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{{ABSTRACT_PUBMED_15514159}}
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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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==About this Structure==
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<div class="pdbe-citations 1w88" style="background-color:#fffaf0;"></div>
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[[1w88]] is a 10 chain structure of [[Dihydrolipoamide acetyltransferase]] and [[Pyruvate dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W88 OCA].
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==See Also==
==See Also==
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*[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]]
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*[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]]
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*[[Pyruvate dehydrogenase|Pyruvate dehydrogenase]]
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*[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015514159</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: Frank, R A.W.]]
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[[Category: Large Structures]]
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[[Category: Luisi, B F.]]
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[[Category: Frank RAW]]
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[[Category: Pei, X Y.]]
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[[Category: Luisi BF]]
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[[Category: Perham, R N.]]
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[[Category: Pei XY]]
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[[Category: Pratap, J V.]]
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[[Category: Perham RN]]
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[[Category: Acetyl transferase]]
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[[Category: Pratap JV]]
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[[Category: Catalysis]]
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[[Category: Dihydrolipoyl]]
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[[Category: Multienzyme complex]]
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[[Category: Oxidoreductase]]
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[[Category: Pyruvate dehydrogenase]]
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[[Category: Slinky]]
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[[Category: Transferase]]
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Current revision

The crystal structure of pyruvate dehydrogenase E1(D180N,E183Q) bound to the peripheral subunit binding domain of E2

PDB ID 1w88

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