6QL5
Structure of fatty acid synthase complex with bound gamma subunit from Saccharomyces cerevisiae at 2.8 angstrom
This is a non-PDB format compatible entry.
Summary for 6QL5
| Entry DOI | 10.2210/pdb6ql5/pdb |
| EMDB information | 4577 |
| Descriptor | Fatty acid synthase subunit alpha, Fatty acid synthase subunit beta, Translation machinery-associated protein 17, ... (5 entities in total) |
| Functional Keywords | fatty acid synthase, acyl carrier protein, ketosynthase, ketoreductase, enoyl reductase, dehydratase, malonyl/palmitoyl transferase, acetyl transferase, phosphopantetheine transferase, transferase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 18 |
| Total formula weight | 2714054.23 |
| Authors | Singh, K.,Graf, B.,Linden, A.,Sautner, V.,Urlaub, H.,Tittmann, K.,Stark, H.,Chari, A. (deposition date: 2019-01-31, release date: 2020-03-18, Last modification date: 2025-04-09) |
| Primary citation | Singh, K.,Graf, B.,Linden, A.,Sautner, V.,Urlaub, H.,Tittmann, K.,Stark, H.,Chari, A. Discovery of a Regulatory Subunit of the Yeast Fatty Acid Synthase. Cell, 180:1130-1143.e20, 2020 Cited by PubMed Abstract: 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 γ subunit of the 2.6 megadalton α-βS. 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 γ 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 γ 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. PubMed: 32160528DOI: 10.1016/j.cell.2020.02.034 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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