8ps2

Asymmetric unit of the yeast fatty acid synthase with ACP at the enoyl reductase domain (FASam sample)

spinqualitylabelsall models 8ps2, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ps2 is a 3 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.9Å Ligands: A3Z, FMN, MLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A, 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. Reconstruction of a fatty acid synthesis cycle from acyl carrier protein and cofactor structural snapshots.,Singh K, Bunzel G, Graf B, Yip KM, Neumann-Schaal M, Stark H, Chari A Cell. 2023 Nov 9;186(23):5054-5067.e16. doi: 10.1016/j.cell.2023.10.009. PMID:37949058 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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