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Direct structural analysis of a single acyl carrier protein domain in fatty acid synthase from the fungus Saccharomyces cerevisiae.
Samani, Elnaz Khalili; Chen, Amy C; Lou, Jennifer W; Dai, David L; Keszei, Alexander F A; Tan, Guihong; Boone, Charles; Grininger, Martin; Mazhab-Jafari, Mohammad T.
Afiliación
  • Samani EK; Department of Medical Biophysics, University of Toronto, Toronto, Canada.
  • Chen AC; Department of Medical Biophysics, University of Toronto, Toronto, Canada.
  • Lou JW; Department of Medical Biophysics, University of Toronto, Toronto, Canada.
  • Dai DL; Department of Medical Biophysics, University of Toronto, Toronto, Canada.
  • Keszei AFA; Department of Medical Biophysics, University of Toronto, Toronto, Canada.
  • Tan G; Princess Margaret Cancer Center, University Health Network, Toronto, Canada.
  • Boone C; Donnelly Centre, Toronto, Canada.
  • Grininger M; Donnelly Centre, Toronto, Canada.
  • Mazhab-Jafari MT; Department of Molecular Genetics, University of Toronto, Toronto, Canada.
Commun Biol ; 7(1): 92, 2024 01 12.
Article en En | MEDLINE | ID: mdl-38216676
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 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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteína Transportadora de Acilo Límite: Animals Idioma: En Revista: Commun Biol Año: 2024 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteína Transportadora de Acilo Límite: Animals Idioma: En Revista: Commun Biol Año: 2024 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Reino Unido