6QL5

Structure of fatty acid synthase complex with bound gamma subunit from Saccharomyces cerevisiae at 2.8 angstrom

これはPDB形式変換不可エントリーです。

6QL5 の概要

• エントリーDOI: 10.2210/pdb6ql5/pdb
• EMDBエントリー: 4577
• 分子名称: Fatty acid synthase subunit alpha, Fatty acid synthase subunit beta, Translation machinery-associated protein 17, ... (5 entities in total)
• 機能のキーワード: fatty acid synthase, acyl carrier protein, ketosynthase, ketoreductase, enoyl reductase, dehydratase, malonyl/palmitoyl transferase, acetyl transferase, phosphopantetheine transferase, transferase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 2714054.23

構造登録者

Singh, K.,Graf, B.,Linden, A.,Sautner, V.,Urlaub, H.,Tittmann, K.,Stark, H.,Chari, A. (登録日: 2019-01-31, 公開日: 2020-03-18, 最終更新日: 2020-04-08)

主引用文献

Singh, K.,Graf, B.,Linden, A.,Sautner, V.,Urlaub, H.,Tittmann, K.,Stark, H.,Chari, A.
Discovery of a Regulatory Subunit of the Yeast Fatty Acid Synthase.
Cell, 180:1130-1143.e20, 2020

PubMed Abstract: Fatty acid synthases (FASs) are central to metabolism but are also of biotechnological interest for the production of fine chemicals and biofuels from renewable resources. During fatty acid synthesis, the growing fatty acid chain is thought to be shuttled by the dynamic acyl carrier protein domain to several enzyme active sites. Here, we report the discovery of a γ subunit of the 2.6 megadalton α-βS. cerevisiae FAS, which is shown by high-resolution structures to stabilize a rotated FAS conformation and rearrange ACP domains from equatorial to axial positions. The γ subunit spans the length of the FAS inner cavity, impeding reductase activities of FAS, regulating NADPH turnover by kinetic hysteresis at the ketoreductase, and suppressing off-pathway reactions at the enoylreductase. The γ subunit delineates the functional compartment within FAS. As a scaffold, it may be exploited to incorporate natural and designed enzymatic activities that are not present in natural FAS.

PubMed: 32160528
DOI: 10.1016/j.cell.2020.02.034

実験手法

ELECTRON MICROSCOPY (2.8 Å)