1EK4
BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I IN COMPLEX WITH DODECANOIC ACID TO 1.85 RESOLUTION
1EK4 の概要
| エントリーDOI | 10.2210/pdb1ek4/pdb |
| 関連するPDBエントリー | 1dd8 |
| 分子名称 | BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I, LAURIC ACID (3 entities in total) |
| 機能のキーワード | fatty acid synthase, thiolase fold, claisen condensation, fatty acid substrate complex, transferase |
| 由来する生物種 | Escherichia coli |
| 細胞内の位置 | Cytoplasm: P0A953 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 177096.10 |
| 構造登録者 | Olsen, J.G.,Kadziola, A.,Siggaard-Andersen, M.,von Wettstein-Knowles, P.,Larsen, S. (登録日: 2000-03-06, 公開日: 2001-04-11, 最終更新日: 2024-10-30) |
| 主引用文献 | Olsen, J.G.,Kadziola, A.,von Wettstein-Knowles, P.,Siggaard-Andersen, M.,Larsen, S. Structures of beta-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery. Structure, 9:233-243, 2001 Cited by PubMed Abstract: beta-ketoacyl-acyl carrier protein synthase (KAS) I is vital for the construction of the unsaturated fatty acid carbon skeletons characterizing E. coli membrane lipids. The new carbon-carbon bonds are created by KAS I in a Claisen condensation performed in a three-step enzymatic reaction. KAS I belongs to the thiolase fold enzymes, of which structures are known for five other enzymes. PubMed: 11286890DOI: 10.1016/S0969-2126(01)00583-4 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.85 Å) |
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