2j9f

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[[Image:2j9f.png|left|200px]]
 
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==Human branched-chain alpha-ketoacid dehydrogenase-decarboxylase E1b==
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The line below this paragraph, containing "STRUCTURE_2j9f", creates the "Structure Box" on the page.
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<StructureSection load='2j9f' size='340' side='right'caption='[[2j9f]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2j9f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J9F 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]] 1.88&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=THV:C2-1-HYDROXY-3-METHYL-PROPYL-THIAMIN+DIPHOSPHATE'>THV</scene></td></tr>
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{{STRUCTURE_2j9f| PDB=2j9f | SCENE= }}
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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=2j9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9f OCA], [https://pdbe.org/2j9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j9f RCSB], [https://www.ebi.ac.uk/pdbsum/2j9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j9f ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN] Defects in BCKDHA are a cause of maple syrup urine disease type IA (MSUD1A) [MIM:[https://omim.org/entry/248600 248600]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:2060625</ref> <ref>PMID:8037208</ref> <ref>PMID:2703538</ref> <ref>PMID:2241958</ref> <ref>PMID:1867199</ref> <ref>PMID:1885764</ref> <ref>PMID:8161368</ref> <ref>PMID:7883996</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN] 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/j9/2j9f_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=2j9f 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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A long standing controversy is whether an alternating activesite mechanism occurs during catalysis in thiamine diphosphate (ThDP)-dependent enzymes. We address this question by investigating the ThDP-dependent decarboxylase/dehydrogenase (E1b) component of the mitochondrial branched-chain alpha-keto acid dehydrogenase complex (BCKDC). Our crystal structure reveals that conformations of the two active sites in the human E1b heterotetramer harboring the reaction intermediate are identical. Acidic residues in the core of the E1b heterotetramer, which align with the proton-wire residues proposed to participate in active-site communication in the related pyruvate dehydrogenase from Bacillus stearothermophilus, are mutated. Enzyme kinetic data show that, except in a few cases because of protein misfolding, these alterations are largely without effect on overall activity of BCKDC, ruling out the requirement of a proton-relay mechanism in E1b. BCKDC overall activity is nullified at 50% phosphorylation of E1b, but it is restored to nearly half of the pre-phosphorylation level after dissociation and reconstitution of BCKDC with the same phosphorylated E1b. The results suggest that the abolition of overall activity likely results from the specific geometry of the half-phosphorylated E1b in the BCKDC assembly and not due to a disruption of the alternating active-site mechanism. Finally, we show that a mutant E1b containing only one functional active site exhibits half of the wild-type BCKDC activity, which directly argues against the obligatory communication between active sites. The above results provide evidence that the two active sites in the E1b heterotetramer operate independently during the ThDP-dependent decarboxylation reaction.
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===HUMAN BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE-DECARBOXYLASE E1B===
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The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism.,Li J, Machius M, Chuang JL, Wynn RM, Chuang DT J Biol Chem. 2007 Apr 20;282(16):11904-13. Epub 2007 Feb 27. PMID:17329260<ref>PMID:17329260</ref>
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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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<div class="pdbe-citations 2j9f" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15166214}}, adds the Publication Abstract to the page
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*[[2-oxoisovalerate dehydrogenase 3D structures|2-oxoisovalerate dehydrogenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15166214 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15166214}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2j9f]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J9F OCA].
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==Reference==
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<ref group="xtra">PMID:15166214</ref><ref group="xtra">PMID:11069910</ref><ref group="xtra">PMID:16472748</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Chuang, D T.]]
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[[Category: Large Structures]]
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[[Category: Chuang, J L.]]
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[[Category: Chuang DT]]
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[[Category: Jun, L.]]
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[[Category: Chuang JL]]
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[[Category: Machius, M.]]
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[[Category: Jun L]]
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[[Category: Wynn, R M.]]
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[[Category: Machius M]]
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[[Category: Branched-chain]]
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[[Category: Wynn RM]]
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[[Category: Disease mutation]]
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[[Category: Flavoprotein]]
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[[Category: Ketoacid dehydrogenase]]
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[[Category: Maple syrup urine disease]]
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[[Category: Metal-binding]]
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[[Category: Mitochondrion]]
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[[Category: Multi-enzyme complex]]
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[[Category: Oxidoreductase]]
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[[Category: Phosphorylation]]
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[[Category: Potassium]]
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[[Category: Thiamine pyrophosphate]]
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[[Category: Transit peptide]]
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Current revision

Human branched-chain alpha-ketoacid dehydrogenase-decarboxylase E1b

PDB ID 2j9f

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