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5zqz

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Current revision (10:28, 27 March 2024) (edit) (undo)
 
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<SX load='5zqz' size='340' side='right' viewer='molstar' caption='[[5zqz]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
<SX load='5zqz' size='340' side='right' viewer='molstar' caption='[[5zqz]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5zqz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZQZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZQZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5zqz]] 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=5ZQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZQZ FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HADHA, HADH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HADHB, MSTP029 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acyltransferase Acetyl-CoA C-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.16 2.3.1.16] </span></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=5zqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zqz OCA], [https://pdbe.org/5zqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zqz RCSB], [https://www.ebi.ac.uk/pdbsum/5zqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zqz ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zqz OCA], [http://pdbe.org/5zqz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zqz RCSB], [http://www.ebi.ac.uk/pdbsum/5zqz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zqz ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/ECHA_HUMAN ECHA_HUMAN]] Mitochondrial trifunctional protein deficiency;Acute fatty liver of pregnancy;Long chain 3-hydroxyacyl-CoA dehydrogenase deficiency. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/ECHB_HUMAN ECHB_HUMAN]] Mitochondrial trifunctional protein deficiency. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/ECHA_HUMAN ECHA_HUMAN] Mitochondrial trifunctional protein deficiency;Acute fatty liver of pregnancy;Long chain 3-hydroxyacyl-CoA dehydrogenase deficiency. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ECHA_HUMAN ECHA_HUMAN]] Bifunctional subunit.
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[https://www.uniprot.org/uniprot/ECHA_HUMAN ECHA_HUMAN] Bifunctional subunit.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The mitochondrial trifunctional protein (TFP) catalyzes three reactions in the fatty acid beta-oxidation process. Mutations in the two TFP subunits cause mitochondrial trifunctional protein deficiency and acute fatty liver of pregnancy that can lead to death. Here we report a 4.2-A cryo-electron microscopy alpha2beta2 tetrameric structure of the human TFP. The tetramer has a V-shaped architecture that displays a distinct assembly compared with the bacterial TFPs. A concave surface of the TFP tetramer interacts with the detergent molecules in the structure, suggesting that this region is involved in associating with the membrane. Deletion of a helical hairpin in TFPbeta decreases its binding to the liposomes in vitro and reduces its membrane targeting in cells. Our results provide the structural basis for TFP function and have important implications for fatty acid oxidation related diseases.
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Cryo-EM structure of human mitochondrial trifunctional protein.,Liang K, Li N, Wang X, Dai J, Liu P, Wang C, Chen XW, Gao N, Xiao J Proc Natl Acad Sci U S A. 2018 Jun 18. pii: 1801252115. doi:, 10.1073/pnas.1801252115. PMID:29915090<ref>PMID:29915090</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 5zqz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
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[[Category: Acetyl-CoA C-acyltransferase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, X]]
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[[Category: Chen X]]
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[[Category: Dai, J]]
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[[Category: Dai J]]
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[[Category: Gao, N]]
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[[Category: Gao N]]
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[[Category: Li, N]]
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[[Category: Li N]]
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[[Category: Liang, K]]
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[[Category: Liang K]]
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[[Category: Liu, P]]
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[[Category: Liu P]]
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[[Category: Wang, C]]
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[[Category: Wang C]]
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[[Category: Wang, X]]
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[[Category: Wang X]]
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[[Category: Xiao, J]]
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[[Category: Xiao J]]
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[[Category: Cryo-em single-particle reconstruction]]
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[[Category: Fatty acid beta-oxidation]]
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[[Category: Hydrolase-transferase complex]]
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[[Category: Lyase]]
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[[Category: Mitochondrial trifunctional protein]]
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Current revision

Structure of human mitochondrial trifunctional protein, tetramer

5zqz, resolution 4.20Å

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