2CF2

Architecture of mammalian fatty acid synthase

2CF2 の概要

• エントリーDOI: 10.2210/pdb2cf2/pdb
• 関連するPDBエントリー: 2CDH
• 分子名称: FATTY ACID SYNTHASE, KS DOMAIN, FATTY ACID SYNTHASE, MAT DOMAIN, FATTY ACID SYNTHASE, DH DOMAIN, ... (5 entities in total)
• 機能のキーワード: transferase, fatty acid metabolism, fatty acid biosynthesis, multienzyme
• 由来する生物種: SUS SCROFA (PIG); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 333132.67

構造登録者

Maier, T.,Jenni, S.,Ban, N. (登録日: 2006-02-14, 公開日: 2006-03-07, 最終更新日: 2024-05-08)

主引用文献

Maier, T.,Jenni, S.,Ban, N.
Architecture of Mammalian Fatty Acid Synthase at 4.5 A Resolution.
Science, 311:1258-, 2006

PubMed Abstract: The homodimeric mammalian fatty acid synthase is one of the most complex cellular multienzymes, in that each 270-kilodalton polypeptide chain carries all seven functional domains required for fatty acid synthesis. We have calculated a 4.5 angstrom-resolution x-ray crystallographic map of porcine fatty acid synthase, highly homologous to the human multienzyme, and placed homologous template structures of all individual catalytic domains responsible for the cyclic elongation of fatty acid chains into the electron density. The positioning of domains reveals the complex architecture of the multienzyme forming an intertwined dimer with two lateral semicircular reaction chambers, each containing a full set of catalytic domains required for fatty acid elongation. Large distances between active sites and conformational differences between the reaction chambers demonstrate that mobility of the acyl carrier protein and general flexibility of the multienzyme must accompany handover of the reaction intermediates during the reaction cycle.

PubMed: 16513975
DOI: 10.1126/SCIENCE.1123248

実験手法

X-RAY DIFFRACTION (4.3 Å)