6ql5: Difference between revisions
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The | ==Structure of fatty acid synthase complex with bound gamma subunit from Saccharomyces cerevisiae at 2.8 angstrom== | ||
<StructureSection load='6ql5' size='340' side='right'caption='[[6ql5]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ql5]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QL5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QL5 FirstGlance]. <br> | |||
</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'>[http://proteopedia.org/fgij/fg.htm?mol=6ql5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ql5 OCA], [http://pdbe.org/6ql5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ql5 RCSB], [http://www.ebi.ac.uk/pdbsum/6ql5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ql5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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] [[http://www.uniprot.org/uniprot/TMA17_YEAST TMA17_YEAST]] ATPase-dedicated chaperone that assists the formation of the RPT6-RPT3 ATPase pair, an early step in proteasome assembly. Plays a key role in maintaining homeostatic proteasome levels and adjusting proteasome assembly when demands increase, such as during proteasome stresses. Function overlaps with RPN14.<ref>PMID:25042801</ref> [[http://www.uniprot.org/uniprot/FAS1_YEAST FAS1_YEAST]] 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. | |||
<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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ql5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | |||
[[Category: Chari, A]] | |||
[[Category: Graf, B]] | |||
[[Category: Linden, A]] | |||
[[Category: Sautner, V]] | |||
[[Category: Singh, K]] | |||
[[Category: Stark, H]] | |||
[[Category: Tittmann, K]] | |||
[[Category: Urlaub, H]] | |||
[[Category: Acetyl transferase]] | |||
[[Category: Acyl carrier protein]] | |||
[[Category: Dehydratase]] | |||
[[Category: Enoyl reductase]] | |||
[[Category: Fatty acid synthase]] | |||
[[Category: Ketoreductase]] | |||
[[Category: Ketosynthase]] | |||
[[Category: Malonyl/palmitoyl transferase]] | |||
[[Category: Phosphopantetheine transferase]] | |||
[[Category: Transferase]] | |||
Latest revision as of 10:20, 8 April 2020
Structure of fatty acid synthase complex with bound gamma subunit from Saccharomyces cerevisiae at 2.8 angstromStructure of fatty acid synthase complex with bound gamma subunit from Saccharomyces cerevisiae at 2.8 angstrom
Structural highlights
Function[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] [TMA17_YEAST] ATPase-dedicated chaperone that assists the formation of the RPT6-RPT3 ATPase pair, an early step in proteasome assembly. Plays a key role in maintaining homeostatic proteasome levels and adjusting proteasome assembly when demands increase, such as during proteasome stresses. Function overlaps with RPN14.[1] [FAS1_YEAST] 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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