1t9g

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{{STRUCTURE_1t9g| PDB=1t9g | SCENE= }}
 
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===Structure of the human MCAD:ETF complex===
 
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{{ABSTRACT_PUBMED_15159392}}
 
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==Disease==
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==Structure of the human MCAD:ETF complex==
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[[http://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[http://omim.org/entry/201450 201450]]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref><ref>PMID:2394825</ref><ref>PMID:2251268</ref><ref>PMID:1684086</ref><ref>PMID:1902818</ref><ref>PMID:1671131</ref><ref>PMID:8198141</ref><ref>PMID:7603790</ref><ref>PMID:7929823</ref><ref>PMID:9158144</ref><ref>PMID:9882619</ref><ref>PMID:10767181</ref><ref>PMID:11349232</ref><ref>PMID:11409868</ref><ref>PMID:11486912</ref> [[http://www.uniprot.org/uniprot/ETFB_HUMAN ETFB_HUMAN]] Defects in ETFB are the cause of glutaric aciduria type 2B (GA2B) [MIM:[http://omim.org/entry/231680 231680]]. GA2B is an autosomal recessively inherited disorder of fatty acid, amino acid, and choline metabolism. It is characterized by multiple acyl-CoA dehydrogenase deficiencies resulting in large excretion not only of glutaric acid, but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids.<ref>PMID:12815589</ref><ref>PMID:7912128</ref> [[http://www.uniprot.org/uniprot/ETFA_HUMAN ETFA_HUMAN]] Defects in ETFA are the cause of glutaric aciduria type 2A (GA2A) [MIM:[http://omim.org/entry/231680 231680]]; also known as glutaricaciduria IIA. GA2A is an autosomal recessively inherited disorder of fatty acid, amino acid, and choline metabolism. It is characterized by multiple acyl-CoA dehydrogenase deficiencies resulting in large excretion not only of glutaric acid, but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids.<ref>PMID:1882842</ref><ref>PMID:1430199</ref>
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<StructureSection load='1t9g' size='340' side='right'caption='[[1t9g]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[1t9g]] is a 6 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=1T9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T9G FirstGlance]. <br>
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[[http://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] This enzyme is specific for acyl chain lengths of 4 to 16. [[http://www.uniprot.org/uniprot/ETFB_HUMAN ETFB_HUMAN]] The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). [[http://www.uniprot.org/uniprot/ETFA_HUMAN ETFA_HUMAN]] The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).
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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]] 2.9&#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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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==About this Structure==
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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=1t9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t9g OCA], [https://pdbe.org/1t9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t9g RCSB], [https://www.ebi.ac.uk/pdbsum/1t9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t9g ProSAT]</span></td></tr>
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[[1t9g]] is a 6 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=1T9G OCA].
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[https://omim.org/entry/201450 201450]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref> <ref>PMID:2394825</ref> <ref>PMID:2251268</ref> <ref>PMID:1684086</ref> <ref>PMID:1902818</ref> <ref>PMID:1671131</ref> <ref>PMID:8198141</ref> <ref>PMID:7603790</ref> <ref>PMID:7929823</ref> <ref>PMID:9158144</ref> <ref>PMID:9882619</ref> <ref>PMID:10767181</ref> <ref>PMID:11349232</ref> <ref>PMID:11409868</ref> <ref>PMID:11486912</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN] This enzyme is specific for acyl chain lengths of 4 to 16.
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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/t9/1t9g_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=1t9g ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Acyl-CoA dehydrogenase|Acyl-CoA dehydrogenase]]
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*[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA 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:015159392</ref><references group="xtra"/><references/>
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__TOC__
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[[Category: Acyl-CoA dehydrogenase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Basran, J.]]
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[[Category: Large Structures]]
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[[Category: Leys, D.]]
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[[Category: Basran J]]
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[[Category: Scrutton, N S.]]
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[[Category: Leys D]]
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[[Category: Sutcliffe, M J.]]
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[[Category: Scrutton NS]]
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[[Category: Thiel, A van.]]
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[[Category: Sutcliffe MJ]]
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[[Category: Toogood, H S.]]
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[[Category: Toogood HS]]
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[[Category: Electron transfer]]
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[[Category: Van Thiel A]]
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[[Category: Electron transport]]
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[[Category: Fatty acid oxidation]]
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[[Category: Human electron transferring flavoprotein]]
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[[Category: Human medium chain acyl coa dehydrogenase]]
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[[Category: Oxidoreductase]]
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[[Category: Protein:protein complex]]
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Current revision

Structure of the human MCAD:ETF complex

PDB ID 1t9g

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