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<StructureSection load='6ql6' size='340' side='right'caption='[[6ql6]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='6ql6' size='340' side='right'caption='[[6ql6]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ql6]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6ql6]] is a 12 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=6QL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QL6 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=J8T:[(3~{R})-4-azanyl-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-butyl]+dihydrogen+phosphate'>J8T</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]] 2.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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=J8T:[(3~{R})-4-azanyl-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-butyl]+dihydrogen+phosphate'>J8T</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=6ql6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ql6 OCA], [https://pdbe.org/6ql6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ql6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ql6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ql6 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == 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 acid synthases (FASs) are central to metabolism but are also of biotechnological interest for the production of fine chemicals and biofuels from renewable resources. During fatty acid synthesis, the growing fatty acid chain is thought to be shuttled by the dynamic acyl carrier protein domain to several enzyme active sites. Here, we report the discovery of a gamma subunit of the 2.6 megadalton alpha6-beta6S. cerevisiae FAS, which is shown by high-resolution structures to stabilize a rotated FAS conformation and rearrange ACP domains from equatorial to axial positions. The gamma subunit spans the length of the FAS inner cavity, impeding reductase activities of FAS, regulating NADPH turnover by kinetic hysteresis at the ketoreductase, and suppressing off-pathway reactions at the enoylreductase. The gamma subunit delineates the functional compartment within FAS. As a scaffold, it may be exploited to incorporate natural and designed enzymatic activities that are not present in natural FAS. | |||
Discovery of a Regulatory Subunit of the Yeast Fatty Acid Synthase.,Singh K, Graf B, Linden A, Sautner V, Urlaub H, Tittmann K, Stark H, Chari A Cell. 2020 Mar 4. pii: S0092-8674(20)30211-7. doi: 10.1016/j.cell.2020.02.034. PMID:32160528<ref>PMID:32160528</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ql6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Chari | [[Category: Chari A]] | ||
[[Category: Graf | [[Category: Graf B]] | ||
[[Category: Linden | [[Category: Linden A]] | ||
[[Category: Sautner | [[Category: Sautner V]] | ||
[[Category: Singh | [[Category: Singh K]] | ||
[[Category: Stark | [[Category: Stark H]] | ||
[[Category: Tittmann | [[Category: Tittmann K]] | ||
[[Category: Urlaub | [[Category: Urlaub H]] | ||
Latest revision as of 16:03, 6 November 2024
Structure of Fatty acid synthase complex from Saccharomyces cerevisiae at 2.9 AngstromStructure of Fatty acid synthase complex from Saccharomyces cerevisiae at 2.9 Angstrom
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 acid synthases (FASs) are central to metabolism but are also of biotechnological interest for the production of fine chemicals and biofuels from renewable resources. During fatty acid synthesis, the growing fatty acid chain is thought to be shuttled by the dynamic acyl carrier protein domain to several enzyme active sites. Here, we report the discovery of a gamma subunit of the 2.6 megadalton alpha6-beta6S. cerevisiae FAS, which is shown by high-resolution structures to stabilize a rotated FAS conformation and rearrange ACP domains from equatorial to axial positions. The gamma subunit spans the length of the FAS inner cavity, impeding reductase activities of FAS, regulating NADPH turnover by kinetic hysteresis at the ketoreductase, and suppressing off-pathway reactions at the enoylreductase. The gamma subunit delineates the functional compartment within FAS. As a scaffold, it may be exploited to incorporate natural and designed enzymatic activities that are not present in natural FAS. Discovery of a Regulatory Subunit of the Yeast Fatty Acid Synthase.,Singh K, Graf B, Linden A, Sautner V, Urlaub H, Tittmann K, Stark H, Chari A Cell. 2020 Mar 4. pii: S0092-8674(20)30211-7. doi: 10.1016/j.cell.2020.02.034. PMID:32160528[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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