5I87

Crystal structure of BT-CD domains of human acetyl-CoA carboxylase

Summary for 5I87

• Entry DOI: 10.2210/pdb5i87/pdb
• Related: 5i6e 5i6f 5i6g 5i6h 5i6i
• Descriptor: BT-CD domains of human acetyl-CoA carboxylase, CADMIUM ION (3 entities in total)
• Functional Keywords: carboxylase, carrier protein-dependent enzyme, fatty acid metabolism, multienzyme, ligase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 118468.37

Authors

Stuttfeld, E.,Hunkeler, M.,Hagmann, A.,Imseng, S.,Maier, T. (deposition date: 2016-02-18, release date: 2016-04-20, Last modification date: 2024-11-13)

Primary citation

Hunkeler, M.,Stuttfeld, E.,Hagmann, A.,Imseng, S.,Maier, T.
The dynamic organization of fungal acetyl-CoA carboxylase.
Nat Commun, 7:11196-11196, 2016

PubMed 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.

PubMed: 27073141
DOI: 10.1038/ncomms11196

Experimental method

X-RAY DIFFRACTION (3.7 Å)