1X2H

Crystal Structure of Lipate-Protein Ligase A from Escherichia coli complexed with lipoic acid

1X2H の概要

• エントリーDOI: 10.2210/pdb1x2h/pdb
• 関連するPDBエントリー: 1X2G
• 分子名称: Lipoate-protein ligase A, LIPOIC ACID (3 entities in total)
• 機能のキーワード: lipoate-protein ligase, lipoic acid, protein acylation, post-translational modification, ligase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P32099
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 114637.95

構造登録者

Fujiwara, K.,Toma, S.,Okamura-Ikeda, K.,Motokawa, Y.,Nakagawa, A.,Taniguchi, H. (登録日: 2005-04-23, 公開日: 2005-08-02, 最終更新日: 2024-10-16)

主引用文献

Fujiwara, K.,Toma, S.,Okamura-Ikeda, K.,Motokawa, Y.,Nakagawa, A.,Taniguchi, H.
Crystal structure of lipoate-protein ligase A from Escherichia coli: Determination of the lipoic acid-binding site
J.Biol.Chem., 280:33645-33651, 2005

PubMed Abstract: Lipoate-protein ligase A (LplA) catalyzes the formation of lipoyl-AMP from lipoate and ATP and then transfers the lipoyl moiety to a specific lysine residue on the acyltransferase subunit of alpha-ketoacid dehydrogenase complexes and on H-protein of the glycine cleavage system. The lypoyllysine arm plays a pivotal role in the complexes by shuttling the reaction intermediate and reducing equivalents between the active sites of the components of the complexes. We have determined the X-ray crystal structures of Escherichia coli LplA alone and in a complex with lipoic acid at 2.4 and 2.9 angstroms resolution, respectively. The structure of LplA consists of a large N-terminal domain and a small C-terminal domain. The structure identifies the substrate binding pocket at the interface between the two domains. Lipoic acid is bound in a hydrophobic cavity in the N-terminal domain through hydrophobic interactions and a weak hydrogen bond between carboxyl group of lipoic acid and the Ser-72 or Arg-140 residue of LplA. No large conformational change was observed in the main chain structure upon the binding of lipoic acid.

PubMed: 16043486
DOI: 10.1074/jbc.M505010200

実験手法

X-RAY DIFFRACTION (2.91 Å)