1F7T
HOLO-(ACYL CARRIER PROTEIN) SYNTHASE AT 1.8A
1F7T の概要
| エントリーDOI | 10.2210/pdb1f7t/pdb |
| 関連するPDBエントリー | 1F7L |
| 分子名称 | HOLO-(ACYL CARRIER PROTEIN) SYNTHASE, SODIUM ION, CHLORIDE ION, ... (6 entities in total) |
| 機能のキーワード | 9-strand pseudo beta barrel, lipid synthesis, transferase |
| 由来する生物種 | Bacillus subtilis |
| 細胞内の位置 | Cytoplasm : P96618 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 83963.05 |
| 構造登録者 | Parris, K.D.,Lin, L.,Tam, A.,Mathew, R.,Hixon, J.,Stahl, M.,Fritz, C.C.,Seehra, J.,Somers, W.S. (登録日: 2000-06-27, 公開日: 2001-06-27, 最終更新日: 2024-02-07) |
| 主引用文献 | Parris, K.D.,Lin, L.,Tam, A.,Mathew, R.,Hixon, J.,Stahl, M.,Fritz, C.C.,Seehra, J.,Somers, W.S. Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Structure Fold.Des., 8:883-895, 2000 Cited by PubMed Abstract: Holo-(acyl carrier protein) synthase (AcpS), a member of the phosphopantetheinyl transferase superfamily, plays a crucial role in the functional activation of acyl carrier protein (ACP) in the fatty acid biosynthesis pathway. AcpS catalyzes the attachment of the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to the sidechain of a conserved serine residue on apo-ACP. PubMed: 10997907DOI: 10.1016/S0969-2126(00)00178-7 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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