5i6h | pdb_00005i6h

Crystal structure of CD-CT domains of Chaetomium thermophilum acetyl-CoA carboxylase

spinqualitylabelsall models 5i6h, resolution 7.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5i6h is a 2 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 7.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0S3L5_CHATD Publication Abstract from PubMed 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. The dynamic organization of fungal acetyl-CoA carboxylase.,Hunkeler M, Stuttfeld E, Hagmann A, Imseng S, Maier T Nat Commun. 2016 Apr 13;7:11196. doi: 10.1038/ncomms11196. PMID:27073141 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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