8phe: Difference between revisions

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'''Unreleased structure'''


The entry 8phe is ON HOLD  until Paper Publication
==ACAD9-WT in complex with ECSIT-CTER==
 
<StructureSection load='8phe' size='340' side='right'caption='[[8phe]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
Authors: McGregor, L., Acajjaoui, S., Desfosses, A., Saidi, M., Bacia-Verloop, M., Schwarz, J.J., Juyoux, P., Von Velsen, J., Bowler, M.W., McCarthy, A., Kandiah, E., Gutsche, I., Soler-Lopez, M.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[8phe]] 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=8PHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PHE FirstGlance]. <br>
Description: ACAD9-WT in complex with ECSIT-CTER
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8phe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8phe OCA], [https://pdbe.org/8phe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8phe RCSB], [https://www.ebi.ac.uk/pdbsum/8phe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8phe ProSAT]</span></td></tr>
[[Category: Bacia-Verloop, M]]
</table>
[[Category: Mccarthy, A]]
== Disease ==
[[Category: Schwarz, J.J]]
[https://www.uniprot.org/uniprot/ACAD9_HUMAN ACAD9_HUMAN] Acyl-CoA dehydrogenase 9 deficiency. The disease is caused by variants affecting the gene represented in this entry.
[[Category: Von Velsen, J]]
== Function ==
[[Category: Bowler, M.W]]
[https://www.uniprot.org/uniprot/ACAD9_HUMAN ACAD9_HUMAN] As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation (PubMed:20816094, PubMed:24158852, PubMed:32320651). This moonlighting protein has also a dehydrogenase activity toward a broad range of substrates with greater specificity for long-chain unsaturated acyl-CoAs (PubMed:12359260, PubMed:16020546, PubMed:21237683, PubMed:24158852). However, in vivo, it does not seem to play a primary role in fatty acid oxidation (PubMed:20816094, PubMed:24158852). In addition, the function in complex I assembly is independent of the dehydrogenase activity of the protein (PubMed:24158852).<ref>PMID:12359260</ref> <ref>PMID:16020546</ref> <ref>PMID:20816094</ref> <ref>PMID:21237683</ref> <ref>PMID:24158852</ref> <ref>PMID:32320651</ref>
[[Category: Soler-Lopez, M]]
== References ==
[[Category: Gutsche, I]]
<references/>
[[Category: Kandiah, E]]
__TOC__
[[Category: Mcgregor, L]]
</StructureSection>
[[Category: Desfosses, A]]
[[Category: Homo sapiens]]
[[Category: Saidi, M]]
[[Category: Large Structures]]
[[Category: Acajjaoui, S]]
[[Category: Acajjaoui S]]
[[Category: Juyoux, P]]
[[Category: Bacia-Verloop M]]
[[Category: Bowler MW]]
[[Category: Desfosses A]]
[[Category: Gutsche I]]
[[Category: Juyoux P]]
[[Category: Kandiah E]]
[[Category: McCarthy A]]
[[Category: McGregor L]]
[[Category: Saidi M]]
[[Category: Schwarz JJ]]
[[Category: Soler-Lopez M]]
[[Category: Von Velsen J]]
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