5I6H

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

5I6H の概要

• エントリーDOI: 10.2210/pdb5i6h/pdb
• 関連するPDBエントリー: 5i6e 5i6f 5i6g 5i6i 5i87
• 分子名称: Acetyl-CoA carboxylase-like protein (1 entity in total)
• 機能のキーワード: carboxylase, fatty acid metabolism, multienzyme, carrier protein-dependent enzyme, ligase
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 338660.12

構造登録者

Hunkeler, M.,Stuttfeld, E.,Hagmann, A.,Imseng, S.,Maier, T. (登録日: 2016-02-16, 公開日: 2016-04-20, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (7.2 Å)