1L0H

CRYSTAL STRUCTURE OF BUTYRYL-ACP FROM E.COLI

1L0H の概要

• エントリーDOI: 10.2210/pdb1l0h/pdb
• 関連するPDBエントリー: 1L0I
• 分子名称: ACYL CARRIER PROTEIN, ZINC ION (3 entities in total)
• 機能のキーワード: acyl carrier protein, acyl chain binding, fatty acid biosynthesis, lipid transport
• 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: 1
• 化学式量合計: 8776.28

構造登録者

Roujeinikova, A.,Baldock, C.,Simon, W.J.,Gilroy, J.,Baker, P.J.,Stuitje, A.R.,Rice, D.W.,Slabas, A.R.,Rafferty, J.B. (登録日: 2002-02-11, 公開日: 2003-02-11, 最終更新日: 2023-08-16)

主引用文献

Roujeinikova, A.,Baldock, C.,Simon, W.J.,Gilroy, J.,Baker, P.J.,Stuitje, A.R.,Rice, D.W.,Slabas, A.R.,Rafferty, J.B.
X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site
Structure, 10:825-835, 2002

PubMed Abstract: Acyl carrier protein (ACP) is an essential cofactor in biosynthesis of fatty acids and many other reactions that require acyl transfer steps. We have determined the first crystal structures of an acylated form of ACP from E. coli, that of butyryl-ACP. Our analysis of the molecular surface of ACP reveals a plastic hydrophobic cavity in the vicinity of the phosphopantethylated Ser36 residue that is expanded and occupied by the butyryl and beta-mercaptoethylamine moieties of the acylated 4'-phosphopantetheine group in one of our crystal forms. In the other form, the cavity is contracted, and we propose that the protein has adopted the conformation after delivery of substrate into the active site of a partner enzyme.

PubMed: 12057197
DOI: 10.1016/S0969-2126(02)00775-X

実験手法

X-RAY DIFFRACTION (2 Å)