2FVA

Structure of 18:0-ACP with docked fatty acid

2FVA の概要

• エントリーDOI: 10.2210/pdb2fva/pdb
• 関連するPDBエントリー: 2AVA 2fve 2fvf
• NMR情報: BMRB: 6790
• 分子名称: Acyl Carrier Protein, 4'-PHOSPHOPANTETHEINE, STEARIC ACID (3 entities in total)
• 機能のキーワード: 4-helix bundle, biosynthetic protein
• 由来する生物種: Spinacia oleracea (spinach)
• 細胞内の位置: Plastid, chloroplast: P07854
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9487.70

構造登録者

Zornetzer, G.A.,Fox, B.G.,Markley, J.L. (登録日: 2006-01-30, 公開日: 2006-04-11, 最終更新日: 2022-03-09)

主引用文献

Zornetzer, G.A.,Fox, B.G.,Markley, J.L.
Solution structures of spinach acyl carrier protein with decanoate and stearate
Biochemistry, 45:5217-5227, 2006

PubMed Abstract: Acyl carrier protein (ACP) is a cofactor in a variety of biosynthetic pathways, including fatty acid metabolism. Thus, it is of interest to determine structures of physiologically relevant ACP-fatty acid complexes. We report here the NMR solution structures of spinach ACP with decanoate (10:0-ACP) and stearate (18:0-ACP) attached to the 4'-phosphopantetheine prosthetic group. The protein in the fatty acid complexes adopts a single conformer, unlike apo- and holo-ACP, which interconvert in solution between two major conformers. The protein component of both 10:0- and 18:0-ACP adopts the four-helix bundle topology characteristic of ACP, and a fatty acid binding cavity was identified in both structures. Portions of the protein close in space to the fatty acid and the 4'-phosphopantetheine were identified using filtered/edited NOESY experiments. A docking protocol was used to generate protein structures containing bound fatty acid for 10:0- and 18:0-ACP. In both cases, the predominant structure contained fatty acid bound down the center of the helical bundle, in agreement with the location of the fatty acid binding pockets. These structures demonstrate the conformational flexibility of spinach ACP and suggest how the protein changes to accommodate its myriad binding partners.

PubMed: 16618110
DOI: 10.1021/bi052062d

実験手法

SOLUTION NMR