1JJB

A neutral molecule in cation-binding site: Specific binding of PEG-SH to Acetylcholinesterase from Torpedo californica

1JJB の概要

• エントリーDOI: 10.2210/pdb1jjb/pdb
• 関連するPDBエントリー: 1VXR 2ACE
• 分子名称: ACETYLCHOLINESTERASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, 1-DEOXY-1-THIO-HEPTAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: peg (polyethylene), serine hydrolase, alpha/beta hydrolase, neurotransmitter cleavage, catalytic triad, glycosylated protein, hydrolase
• 由来する生物種: Torpedo californica (Pacific electric ray)
• 細胞内の位置: Isoform H: Cell membrane; Lipid-anchor, GPI- anchor. Isoform T: Cell membrane; Peripheral membrane protein: P04058
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60978.84

構造登録者

Koellner, G.,Steiner, T.,Millard, C.B.,Silman, I.,Sussman, J.L. (登録日: 2001-07-04, 公開日: 2002-07-17, 最終更新日: 2024-11-20)

主引用文献

Koellner, G.,Steiner, T.,Millard, C.B.,Silman, I.,Sussman, J.L.
A neutral molecule in a cation-binding site: specific binding of a PEG-SH to acetylcholinesterase from Torpedo californica.
J.Mol.Biol., 320:721-725, 2002

PubMed Abstract: The crystal structure of acetylcholinesterase from Torpedo californica complexed with the uncharged inhibitor, PEG-SH-350 (containing mainly heptameric polyethylene glycol with a terminal thiol group) is determined at 2.3 A resolution. This is an untypical acetylcholinesterase inhibitor, since it lacks the cationic moiety typical of the substrate (acetylcholine). In the crystal structure, the elongated ligand extends along the whole of the deep and narrow active-site gorge, with the terminal thiol group bound near the bottom, close to the catalytic site. Unexpectedly, the cation-binding site (formed by the faces of aromatic side-chains) is occupied by CH(2) groups of the inhibitor, which are engaged in C-H...pi interactions that structurally mimic the cation-pi interactions made by the choline moiety of acetylcholine. In addition, the PEG-SH molecule makes numerous other weak but specific interactions of the C-H...O and C-H...pi types.

PubMed: 12095250
DOI: 10.1016/S0022-2836(02)00475-8

実験手法

X-RAY DIFFRACTION (2.3 Å)