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The dynamic organization of fungal acetyl-CoA carboxylase

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  • Moritz Hunkeler

    (University of Basel)

  • Edward Stuttfeld

    (University of Basel)

  • Anna Hagmann

    (University of Basel)

  • Stefan Imseng

    (University of Basel)

  • Timm Maier

    (University of Basel)

Abstract

Acetyl-CoA carboxylases (ACCs) catalyse the committed step in fatty-acid biosynthesis: the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. They are important regulatory hubs for metabolic control and relevant drug targets for the treatment of the metabolic syndrome and cancer. Eukaryotic ACCs are single-chain multienzymes characterized by a large, non-catalytic central domain (CD), whose role in ACC regulation remains poorly characterized. Here we report the crystal structure of the yeast ACC CD, revealing a unique four-domain organization. A regulatory loop, which is phosphorylated at the key functional phosphorylation site of fungal ACC, wedges into a crevice between two domains of CD. Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. In contrast to related carboxylases, large-scale conformational changes are required for substrate turnover, and are mediated by the CD under phosphorylation control.

Suggested Citation

  • Moritz Hunkeler & Edward Stuttfeld & Anna Hagmann & Stefan Imseng & Timm Maier, 2016. "The dynamic organization of fungal acetyl-CoA carboxylase," Nature Communications, Nature, vol. 7(1), pages 1-11, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11196
    DOI: 10.1038/ncomms11196
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