5I6G: Crystal Structure Of C-terminal Variant 2 Of Chaetomium Thermophilum Acetyl-coa Carboxylase

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.
PDB ID: 5I6GDownload
MMDB ID: 138733
PDB Deposition Date: 2016/2/16
Updated in MMDB: 2016/04
Experimental Method:
x-ray diffraction
Resolution: 4.5  Å
Source Organism:
Similar Structures:
Biological Unit for 5I6G: dimeric; determined by author and by software (PISA)
Molecular Components in 5I6G
Label Count Molecule
Proteins (2 molecules)
Acetyl-coa Carboxylase-like Protein,acetyl-coa Carboxylase- Like Protein
Molecule annotation
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Citing MMDB