8psf: Difference between revisions
New page: '''Unreleased structure''' The entry 8psf is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Asymmetric unit of the yeast fatty acid synthase in non-rotated state with ACP at the acetyl transferase domain (FASx sample)== | ||
<StructureSection load='8psf' size='340' side='right'caption='[[8psf]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8psf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8PSF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PSF FirstGlance]. <br> | |||
</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='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=8psf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8psf OCA], [https://pdbe.org/8psf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8psf RCSB], [https://www.ebi.ac.uk/pdbsum/8psf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8psf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST] 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. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fatty acids (FAs) play a central metabolic role in living cells as constituents of membranes, cellular energy reserves, and second messenger precursors. A 2.6 MDa FA synthase (FAS), where the enzymatic reactions and structures are known, is responsible for FA biosynthesis in yeast. Essential in the yeast FAS catalytic cycle is the acyl carrier protein (ACP) that actively shuttles substrates, biosynthetic intermediates, and products from one active site to another. We resolve the S. cerevisiae FAS structure at 1.9 A, elucidating cofactors and water networks involved in their recognition. Structural snapshots of ACP domains bound to various enzymatic domains allow the reconstruction of a full yeast FA biosynthesis cycle. The structural information suggests that each FAS functional unit could accommodate exogenous proteins to incorporate various enzymatic activities, and we show proof-of-concept experiments where ectopic proteins are used to modulate FAS product profiles. | |||
Reconstruction of a fatty acid synthesis cycle from acyl carrier protein and cofactor structural snapshots.,Singh K, Bunzel G, Graf B, Yip KM, Neumann-Schaal M, Stark H, Chari A Cell. 2023 Nov 9;186(23):5054-5067.e16. doi: 10.1016/j.cell.2023.10.009. PMID:37949058<ref>PMID:37949058</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8psf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | |||
[[Category: Bunzel G]] | |||
[[Category: Chari A]] | |||
[[Category: Graf B]] | |||
[[Category: Singh K]] | |||
[[Category: Stark H]] | |||
[[Category: Yip KM]] | |||
Latest revision as of 10:31, 22 November 2023
Asymmetric unit of the yeast fatty acid synthase in non-rotated state with ACP at the acetyl transferase domain (FASx sample)Asymmetric unit of the yeast fatty acid synthase in non-rotated state with ACP at the acetyl transferase domain (FASx sample)
Structural highlights
FunctionFAS2_YEAST 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. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] Publication Abstract from PubMedFatty acids (FAs) play a central metabolic role in living cells as constituents of membranes, cellular energy reserves, and second messenger precursors. A 2.6 MDa FA synthase (FAS), where the enzymatic reactions and structures are known, is responsible for FA biosynthesis in yeast. Essential in the yeast FAS catalytic cycle is the acyl carrier protein (ACP) that actively shuttles substrates, biosynthetic intermediates, and products from one active site to another. We resolve the S. cerevisiae FAS structure at 1.9 A, elucidating cofactors and water networks involved in their recognition. Structural snapshots of ACP domains bound to various enzymatic domains allow the reconstruction of a full yeast FA biosynthesis cycle. The structural information suggests that each FAS functional unit could accommodate exogenous proteins to incorporate various enzymatic activities, and we show proof-of-concept experiments where ectopic proteins are used to modulate FAS product profiles. Reconstruction of a fatty acid synthesis cycle from acyl carrier protein and cofactor structural snapshots.,Singh K, Bunzel G, Graf B, Yip KM, Neumann-Schaal M, Stark H, Chari A Cell. 2023 Nov 9;186(23):5054-5067.e16. doi: 10.1016/j.cell.2023.10.009. PMID:37949058[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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