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8PSM

Asymmetric unit of the yeast fatty acid synthase in the non-rotated state with ACP at the malonyl/palmitoyl transferase domain (FASx sample)

Summary for 8PSM
Entry DOI10.2210/pdb8psm/pdb
EMDB information17856
DescriptorFatty acid synthase subunit alpha, Fatty acid synthase subunit beta, 4'-PHOSPHOPANTETHEINE, ... (4 entities in total)
Functional Keywordsfatty acid synthase, acyl carrier protein, fas, acp, cytosolic protein
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Total number of polymer chains3
Total formula weight644123.91
Authors
Singh, K.,Bunzel, G.,Graf, B.,Yip, K.M.,Stark, H.,Chari, A. (deposition date: 2023-07-13, release date: 2023-11-22)
Primary citationSingh, 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: 37949058
DOI: 10.1016/j.cell.2023.10.009
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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数据于2025-06-25公开中

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