7bc4

Cryo-EM structure of fatty acid synthase (FAS) from Pichia pastoris

spinqualitylabelsall models 7bc4, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7bc4 is a 2 chain structure with sequence from Komagataella phaffii GS115. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.1Å Ligands: FMN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C4QY10_KOMPG Publication Abstract from PubMed Type I fatty acid synthases (FASs) are critical metabolic enzymes which are common targets for bioengineering in the production of biofuels and other products. Serendipitously, we identified FAS as a contaminant in a cryoEM dataset of virus-like particles (VLPs) purified from P. pastoris, an important model organism and common expression system used in protein production. From these data, we determined the structure of P. pastoris FAS to 3.1 A resolution. While the overall organisation of the complex was typical of type I FASs, we identified several differences in both structural and enzymatic domains through comparison with the prototypical yeast FAS from S. cerevisiae. Using focussed classification, we were also able to resolve and model the mobile acyl-carrier protein (ACP) domain, which is key for function. Ultimately, the structure reported here will be a useful resource for further efforts to engineer yeast FAS for synthesis of alternate products. Structural insight into Pichia pastoris fatty acid synthase.,Snowden JS, Alzahrani J, Sherry L, Stacey M, Rowlands DJ, Ranson NA, Stonehouse NJ Sci Rep. 2021 May 7;11(1):9773. doi: 10.1038/s41598-021-89196-2. PMID:33963233 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fatty acid synthase 3D structures

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