2KOO

NMR solution structures of hexanoyl-ACP from the Streptomyces coelicolor Fatty Acid Synthase

2KOO の概要

• エントリーDOI: 10.2210/pdb2koo/pdb
• 関連するPDBエントリー: 2KOP 2KOQ 2KOR 2KOS
• NMR情報: BMRB: 16524
• 分子名称: Acyl carrier protein, S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] hexanethioate (2 entities in total)
• 機能のキーワード: acyl carrier protein, intermediate binding, fatty acid synthase, transport protein
• 由来する生物種: Streptomyces coelicolor
• 細胞内の位置: Cytoplasm (By similarity): P72393
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9250.26

構造登録者

Ploskon, E.,Arthur, C.J.,Crump, M.P. (登録日: 2009-09-29, 公開日: 2010-08-18, 最終更新日: 2024-11-13)

主引用文献

Ploskon, E.,Arthur, C.J.,Kanari, A.L.,Wattana-amorn, P.,Williams, C.,Crosby, J.,Simpson, T.J.,Willis, C.L.,Crump, M.P.
Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis
Chem.Biol., 17:776-785, 2010

PubMed Abstract: It remains unclear whether in a bacterial fatty acid synthase (FAS) acyl chain transfer is a programmed or diffusion controlled and random action. Acyl carrier protein (ACP), which delivers all intermediates and interacts with all synthase enzymes, is the key player in this process. High-resolution structures of intermediates covalently bound to an ACP representing each step in fatty acid biosynthesis have been solved by solution NMR. These include hexanoyl-, 3-oxooctanyl-, 3R-hydroxyoctanoyl-, 2-octenoyl-, and octanoyl-ACP from Streptomyces coelicolor FAS. The high-resolution structures reveal that the ACP adopts a unique conformation for each intermediate driven by changes in the internal fatty acid binding pocket. The binding of each intermediate shows conserved structural features that may ensure effective molecular recognition over subsequent rounds of fatty acid biosynthesis.

PubMed: 20659690
DOI: 10.1016/j.chembiol.2010.05.024

実験手法

SOLUTION NMR