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| | <SX load='6u5v' size='340' side='right' viewer='molstar' caption='[[6u5v]], [[Resolution|resolution]] 2.80Å' scene=''> | | <SX load='6u5v' size='340' side='right' viewer='molstar' caption='[[6u5v]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6u5v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U5V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6u5v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U5V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></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]] 2.8Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6u5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u5v OCA], [http://pdbe.org/6u5v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u5v RCSB], [http://www.ebi.ac.uk/pdbsum/6u5v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u5v ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></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=6u5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u5v OCA], [https://pdbe.org/6u5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u5v RCSB], [https://www.ebi.ac.uk/pdbsum/6u5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u5v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FAS2_CANAX FAS2_CANAX]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. [[http://www.uniprot.org/uniprot/FAS1_CANAX FAS1_CANAX]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase. | + | [https://www.uniprot.org/uniprot/FAS2_CANAX FAS2_CANAX] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6u5v" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6u5v" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Candida albicans]] | | [[Category: Candida albicans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lou, J W]] | + | [[Category: Lou JW]] |
| - | [[Category: Mazhab-Jafari, M T]] | + | [[Category: Mazhab-Jafari MT]] |
| - | [[Category: Fungal fatty acid synthase]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
FAS2_CANAX Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase.
Publication Abstract from PubMed
During fatty acid biosynthesis, acyl carrier proteins (ACPs) from type I fungal fatty acid synthase (FAS) shuttle substrates and intermediates within a reaction chamber that hosts multiple spatially-fixed catalytic centers. A major challenge in understanding the mechanism of ACP-mediated substrate shuttling is experimental observation of its transient interaction landscape within the reaction chamber. Here, we have shown that ACP spatial distribution is sensitive to the presence of substrates in a catalytically inhibited state, which enables high-resolution investigation of the ACP-dependent conformational transitions within the enoyl reductase (ER) reaction site. In two fungal FASs with distinct ACP localization, the shuttling domain is targeted to the ketoacyl-synthase (KS) domain and away from other catalytic centers, such as acetyl-transferase (AT) and ER domains by steric blockage of the KS active site followed by addition of substrates. These studies strongly suggest that acylation of phosphopantetheine arm of ACP may be an integral part of the substrate shuttling mechanism in type I fungal FAS.
Electron cryomicroscopy observation of acyl carrier protein translocation in type I fungal fatty acid synthase.,Lou JW, Iyer KR, Hasan SMN, Cowen LE, Mazhab-Jafari MT Sci Rep. 2019 Sep 10;9(1):12987. doi: 10.1038/s41598-019-49261-3. PMID:31506493[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lou JW, Iyer KR, Hasan SMN, Cowen LE, Mazhab-Jafari MT. Electron cryomicroscopy observation of acyl carrier protein translocation in type I fungal fatty acid synthase. Sci Rep. 2019 Sep 10;9(1):12987. doi: 10.1038/s41598-019-49261-3. PMID:31506493 doi:http://dx.doi.org/10.1038/s41598-019-49261-3
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