8PSJ
Asymmetric unit of the yeast fatty acid synthase in the semi rotated state with ACP at the acetyl transferase domain (FASx sample)
This is a non-PDB format compatible entry.
Summary for 8PSJ
| Entry DOI | 10.2210/pdb8psj/pdb |
| EMDB information | 17853 |
| Descriptor | Fatty acid synthase subunit alpha, Fatty acid synthase subunit beta, 4'-PHOSPHOPANTETHEINE, ... (4 entities in total) |
| Functional Keywords | fatty acid synthase, acyl carrier protein, fas, acp, cytosolic protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 3 |
| Total formula weight | 644123.91 |
| Authors | |
| Primary citation | Singh, K.,Bunzel, G.,Graf, B.,Yip, K.M.,Neumann-Schaal, M.,Stark, H.,Chari, A. Reconstruction of a fatty acid synthesis cycle from acyl carrier protein and cofactor structural snapshots. Cell, 186:5054-5067.e16, 2023 Cited by PubMed Abstract: 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 Å, 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. PubMed: 37949058DOI: 10.1016/j.cell.2023.10.009 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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