8brj
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8brj]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BRJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BRJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[8brj]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BRJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BRJ FirstGlance]. <br> | ||
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8brj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8brj OCA], [https://pdbe.org/8brj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8brj RCSB], [https://www.ebi.ac.uk/pdbsum/8brj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8brj ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.08Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8brj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8brj OCA], [https://pdbe.org/8brj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8brj RCSB], [https://www.ebi.ac.uk/pdbsum/8brj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8brj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/FADI_ECOLI FADI_ECOLI] Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids.<ref>PMID:12270828</ref> <ref>PMID:12535077</ref> | [https://www.uniprot.org/uniprot/FADI_ECOLI FADI_ECOLI] Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids.<ref>PMID:12270828</ref> <ref>PMID:12535077</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Facultative anaerobic bacteria such as Escherichia coli have two alpha(2)beta(2) heterotetrameric trifunctional enzymes (TFE), catalyzing the last three steps of the beta-oxidation cycle: soluble aerobic TFE (EcTFE) and membrane-associated anaerobic TFE (anEcTFE), closely related to the human mitochondrial TFE (HsTFE). The cryo-EM structure of anEcTFE and crystal structures of anEcTFE-alpha show that the overall assembly of anEcTFE and HsTFE is similar. However, their membrane-binding properties differ considerably. The shorter A5-H7 and H8 regions of anEcTFE-alpha result in weaker alpha-beta as well as alpha-membrane interactions, respectively. The protruding H-H region of anEcTFE-beta is therefore more critical for membrane-association. Mutational studies also show that this region is important for the stability of the anEcTFE-beta dimer and anEcTFE heterotetramer. The fatty acyl tail binding tunnel of the anEcTFE-alpha hydratase domain, as in HsTFE-alpha, is wider than in EcTFE-alpha, accommodating longer fatty acyl tails, in good agreement with their respective substrate specificities. | ||
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| + | Structural basis for different membrane-binding properties of E. coli anaerobic and human mitochondrial beta-oxidation trifunctional enzymes.,Sah-Teli SK, Pinkas M, Hynonen MJ, Butcher SJ, Wierenga RK, Novacek J, Venkatesan R Structure. 2023 Jul 6;31(7):812-825.e6. doi: 10.1016/j.str.2023.04.011. Epub 2023 , May 15. PMID:37192613<ref>PMID:37192613</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8brj" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Escherichia coli anaerobic fatty acid beta oxidation trifunctional enzyme (anEcTFE) trimeric complex
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