The dynamic organization of fungal acetyl-CoA carboxylase

Moritz Hunkeler, Edward Stuttfeld, Anna Hagmann, Stefan Imseng and Timm Maier ()
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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

Nature Communications, 2016, vol. 7, issue 1, 1-11

Abstract: 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.

Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11196

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DOI: 10.1038/ncomms11196

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