1qs0

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(New page: 200px<br /><applet load="1qs0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qs0, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1qs0.jpg|left|200px]]<br /><applet load="1qs0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qs0, resolution 2.40&Aring;" />
 
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'''CRYSTAL STRUCTURE OF PSEUDOMONAS PUTIDA 2-OXOISOVALERATE DEHYDROGENASE (BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE, E1B)'''<br />
 
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==Overview==
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==Crystal Structure of Pseudomonas Putida 2-oxoisovalerate Dehydrogenase (Branched-Chain Alpha-Keto Acid Dehydrogenase, E1B)==
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The family of giant multienzyme complexes metabolizing pyruvate, 2-oxoglutarate, branched-chain 2-oxo acids or acetoin contains several of, the largest and most sophisticated protein assemblies known, with, molecular masses between 4 and 10 million Da. The principal enzyme, components, E1, E2 and E3, are present in numerous copies and utilize, multiple cofactors to catalyze a directed sequence of reactions via, substrate channeling. The crystal structure of a heterotetrameric, (alpha2beta2) E1, 2-oxoisovalerate dehydrogenase from Pseudomonas putida, reveals a tightly packed arrangement of the four subunits with the, beta2-dimer held between the jaws of a 'vise' formed by the alpha2-dimer., A long hydrophobic channel, suitable to accommodate the E2 lipoyl-lysine, arm, leads to the active site, which contains the cofactor thiamin, diphosphate (ThDP) and an inhibitor-derived covalent modification of a, histidine side chain. The E1 structure, together with previous structural, information on E2 and E3, completes the picture of the shared, architectural features of these enormous macromolecular assemblies.
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<StructureSection load='1qs0' size='340' side='right'caption='[[1qs0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qs0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QS0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QS0 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]] 2.4&#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=COI:2-OXO-4-METHYLPENTANOIC+ACID'>COI</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1qs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qs0 OCA], [https://pdbe.org/1qs0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qs0 RCSB], [https://www.ebi.ac.uk/pdbsum/1qs0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qs0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ODBB_PSEPU ODBB_PSEPU] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (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/qs/1qs0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1qs0 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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The family of giant multienzyme complexes metabolizing pyruvate, 2-oxoglutarate, branched-chain 2-oxo acids or acetoin contains several of the largest and most sophisticated protein assemblies known, with molecular masses between 4 and 10 million Da. The principal enzyme components, E1, E2 and E3, are present in numerous copies and utilize multiple cofactors to catalyze a directed sequence of reactions via substrate channeling. The crystal structure of a heterotetrameric (alpha2beta2) E1, 2-oxoisovalerate dehydrogenase from Pseudomonas putida, reveals a tightly packed arrangement of the four subunits with the beta2-dimer held between the jaws of a 'vise' formed by the alpha2-dimer. A long hydrophobic channel, suitable to accommodate the E2 lipoyl-lysine arm, leads to the active site, which contains the cofactor thiamin diphosphate (ThDP) and an inhibitor-derived covalent modification of a histidine side chain. The E1 structure, together with previous structural information on E2 and E3, completes the picture of the shared architectural features of these enormous macromolecular assemblies.
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==About this Structure==
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Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes.,Aevarsson A, Seger K, Turley S, Sokatch JR, Hol WG Nat Struct Biol. 1999 Aug;6(8):785-92. PMID:10426958<ref>PMID:10426958</ref>
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1QS0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with MG, COI and TDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QS0 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes., Aevarsson A, Seger K, Turley S, Sokatch JR, Hol WG, Nat Struct Biol. 1999 Aug;6(8):785-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10426958 10426958]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1qs0" style="background-color:#fffaf0;"></div>
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[[Category: Pseudomonas putida]]
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[[Category: Aevarsson, A.]]
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[[Category: Hol, W.G.J.]]
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[[Category: Seger, K.]]
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[[Category: Sokatch, J.R.]]
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[[Category: Turley, S.]]
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[[Category: COI]]
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[[Category: MG]]
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[[Category: TDP]]
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[[Category: heterotetramer]]
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[[Category: thdp cofactor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:56:06 2007''
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==See Also==
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*[[2-oxoisovalerate dehydrogenase 3D structures|2-oxoisovalerate dehydrogenase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudomonas putida]]
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[[Category: Aevarsson A]]
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[[Category: Hol WGJ]]
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[[Category: Seger K]]
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[[Category: Sokatch JR]]
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[[Category: Turley S]]

Current revision

Crystal Structure of Pseudomonas Putida 2-oxoisovalerate Dehydrogenase (Branched-Chain Alpha-Keto Acid Dehydrogenase, E1B)

PDB ID 1qs0

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