6ql9

Structure of Fatty acid synthase complex from Saccharomyces cerevisiae at 2.9 Angstrom

spinqualitylabelsall models 6ql9, resolution 2.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ql9 is a 12 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.82Å Ligands: A2P, ACT, EDO, FMN, J8W, MLI, NA, PGE, PNS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fatty acid synthase 3D structures

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