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1t9g

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(New page: 200px<br /> <applet load="1t9g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t9g, resolution 2.90&Aring;" /> '''Structure of the hu...)
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[[Image:1t9g.gif|left|200px]]<br />
 
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<applet load="1t9g" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1t9g, resolution 2.90&Aring;" />
 
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'''Structure of the human MCAD:ETF complex'''<br />
 
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==Overview==
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==Structure of the human MCAD:ETF complex==
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The crystal structure of the human electron transferring flavoprotein, (ETF).medium chain acyl-CoA dehydrogenase (MCAD) complex reveals a dual, mode of protein-protein interaction, imparting both specificity and, promiscuity in the interaction of ETF with a range of structurally, distinct primary dehydrogenases. ETF partitions the functions of partner, binding and electron transfer between (i) the recognition loop, which acts, as a static anchor at the ETF.MCAD interface, and (ii) the highly mobile, redox active FAD domain. Together, these enable the FAD domain of ETF to, sample a range of conformations, some compatible with fast interprotein, electron transfer. Disorders in amino acid or fatty acid catabolism can be, attributed to mutations at the protein-protein interface. Crucially, complex formation triggers mobility of the FAD domain, an induced disorder, that contrasts with general models of protein-protein interaction by, induced fit mechanisms. The subsequent interfacial motion in the MCAD.ETF, complex is the basis for the interaction of ETF with structurally diverse, protein partners. Solution studies using ETF and MCAD with mutations at, the protein-protein interface support this dynamic model and indicate, ionic interactions between MCAD Glu(212) and ETF Arg alpha(249) are likely, to transiently stabilize productive conformations of the FAD domain, leading to enhanced electron transfer rates between both partners.
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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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<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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</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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<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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</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>
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==Disease==
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==See Also==
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Known diseases associated with this structure: Acyl-CoA dehydrogenase, medium chain, deficiency of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607008 607008]], Glutaricaciduria, type IIA OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=608053 608053]], Glutaricaciduria, type IIB OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=130410 130410]]
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*[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA dehydrogenase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1T9G is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with AMP and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acyl-CoA_dehydrogenase Acyl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.3 1.3.99.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T9G OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex., Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D, J Biol Chem. 2004 Jul 30;279(31):32904-12. Epub 2004 May 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15159392 15159392]
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[[Category: Acyl-CoA dehydrogenase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Basran, J.]]
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[[Category: Basran J]]
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[[Category: Leys, D.]]
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[[Category: Leys D]]
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[[Category: Scrutton, N.S.]]
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[[Category: Scrutton NS]]
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[[Category: Sutcliffe, M.J.]]
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[[Category: Sutcliffe MJ]]
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[[Category: Thiel, A.van.]]
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[[Category: Toogood HS]]
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[[Category: Toogood, H.S.]]
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[[Category: Van Thiel A]]
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[[Category: AMP]]
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[[Category: FAD]]
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[[Category: electron transfer]]
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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: protein:protein complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:22:22 2007''
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Current revision

Structure of the human MCAD:ETF complex

PDB ID 1t9g

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