8PRV

Asymmetric unit of the yeast fatty acid synthase in the non-rotated state with ACP at the ketosreductase domain (FASamn sample)

8PRV の概要

• エントリーDOI: 10.2210/pdb8prv/pdb
• EMDBエントリー: 17839
• 分子名称: Fatty acid synthase subunit alpha, Fatty acid synthase subunit beta, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total)
• 機能のキーワード: fatty acid synthase, acyl carrier protein, fas, acp, cytosolic protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 646548.36

構造登録者

Singh, K.,Bunzel, G.,Graf, B.,Yip, K.M.,Stark, H.,Chari, A. (登録日: 2023-07-12, 公開日: 2023-11-22)

主引用文献

Singh, K.,Bunzel, G.,Graf, B.,Yip, K.M.,Neumann-Schaal, M.,Stark, H.,Chari, A.
Reconstruction of a fatty acid synthesis cycle from acyl carrier protein and cofactor structural snapshots.
Cell, 186:5054-5067.e16, 2023

PubMed Abstract: Fatty acids (FAs) play a central metabolic role in living cells as constituents of membranes, cellular energy reserves, and second messenger precursors. A 2.6 MDa FA synthase (FAS), where the enzymatic reactions and structures are known, is responsible for FA biosynthesis in yeast. Essential in the yeast FAS catalytic cycle is the acyl carrier protein (ACP) that actively shuttles substrates, biosynthetic intermediates, and products from one active site to another. We resolve the S. cerevisiae FAS structure at 1.9 Å, elucidating cofactors and water networks involved in their recognition. Structural snapshots of ACP domains bound to various enzymatic domains allow the reconstruction of a full yeast FA biosynthesis cycle. The structural information suggests that each FAS functional unit could accommodate exogenous proteins to incorporate various enzymatic activities, and we show proof-of-concept experiments where ectopic proteins are used to modulate FAS product profiles.

PubMed: 37949058
DOI: 10.1016/j.cell.2023.10.009

実験手法

ELECTRON MICROSCOPY (2.9 Å)