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Title | Direct structural analysis of a single acyl carrier protein domain in fatty acid synthase from the fungus Saccharomyces cerevisiae. |
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Journal, issue, pages | Commun Biol, Vol. 7, Issue 1, Page 92, Year 2024 |
Publish date | Jan 12, 2024 |
Authors | Elnaz Khalili Samani / Amy C Chen / Jennifer W Lou / David L Dai / Alexander F A Keszei / Guihong Tan / Charles Boone / Martin Grininger / Mohammad T Mazhab-Jafari / |
PubMed Abstract | Acyl carrier protein (ACP) is the work horse of polyketide (PKS) and fatty acid synthases (FAS) and acts as a substrate shuttling domain in these mega enzymes. In fungi, FAS forms a 2.6 MDa symmetric ...Acyl carrier protein (ACP) is the work horse of polyketide (PKS) and fatty acid synthases (FAS) and acts as a substrate shuttling domain in these mega enzymes. In fungi, FAS forms a 2.6 MDa symmetric assembly with six identical copies of FAS1 and FAS2 polypeptides. However, ACP spatial distribution is not restricted by symmetry owing to the long and flexible loops that tether the shuttling domain to its corresponding FAS2 polypeptide. This symmetry breaking has hampered experimental investigation of substrate shuttling route in fungal FAS. Here, we develop a protein engineering and expression method to isolate asymmetric fungal FAS proteins containing odd numbers of ACP domains. Electron cryomicroscopy (cryoEM) observation of the engineered complex reveals a non-uniform distribution of the substrate shuttling domain relative to its corresponding FAS2 polypeptide at 2.9 Å resolution. This work lays the methodological foundation for experimental study of ACP shuttling route in fungi. |
External links | Commun Biol / PubMed:38216676 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.87 - 3.21 Å |
Structure data | EMDB-40783: MBP-tagged fusion fatty acid synthase from S. cerevisiae EMDB-40784: MBP tagged and Mixed chain fatty acid synthase, FAS2_deltaACP EMDB-40785: MBP tagged mixed chain FAS, fusFAS_deltaACP |
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