2FAE

Crystal structure of E. coli decanoyl-ACP

2FAE の概要

• エントリーDOI: 10.2210/pdb2fae/pdb
• 関連するPDBエントリー: 1L0H 1L0I
• 分子名称: Acyl carrier protein, ZINC ION, S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL) DECANETHIOATE, ... (4 entities in total)
• 機能のキーワード: acyl carrier protein, acyl chain binding, fatty acid biosynthesis, biosynthetic protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A6A8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18545.00

構造登録者

Roujeinikova, A. (登録日: 2005-12-07, 公開日: 2006-09-26, 最終更新日: 2025-02-12)

主引用文献

Roujeinikova, A.,Simon, W.J.,Gilroy, J.,Rice, D.W.,Rafferty, J.B.,Slabas, A.R.
Structural Studies of Fatty Acyl-(Acyl Carrier Protein) Thioesters Reveal a Hydrophobic Binding Cavity that Can Expand to Fit Longer Substrates.
J.Mol.Biol., 365:135-145, 2007

PubMed Abstract: A knowledge of the structures of acyl chain loaded species of the acyl carrier protein (ACP) as used in fatty acid biosynthesis and a range of other metabolic events, is essential for a full understanding of the molecular recognition at the heart of these processes. To date the only crystal structure of an acylated species of ACP is that of a butyryl derivative of Escherichia coli ACP. We have now determined the structures of a family of acylated E. coli ACPs of varying acyl chain length. The acyl moiety is attached via a thioester bond to a phosphopantetheine linker that is in turn bound to a serine residue in ACP. The growing acyl chain can be accommodated within a central cavity in the ACP for transport during the elongation stages of lipid synthesis through changes in the conformation of a four alpha-helix bundle. The results not only clarify the means by which a substrate of varying size and complexity is transported in the cell but also suggest a mechanism by which interacting enzymes can recognize the loaded ACP through recognition of surface features including the conformation of the phosphopantetheine linker.

PubMed: 17059829
DOI: 10.1016/j.jmb.2006.09.049

実験手法

X-RAY DIFFRACTION (1.55 Å)