1P0P

Crystal structure of soman-aged human butyryl cholinesterase in complex with the substrate analog butyrylthiocholine

1P0P の概要

• エントリーDOI: 10.2210/pdb1p0p/pdb
• 関連するPDBエントリー: 1P0I 1P0M 1P0Q
• 分子名称: Cholinesterase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• 機能のキーワード: serine hydrolase, organophosphates, soman, butyrylthiocholine, cholinesterase, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 62046.62

構造登録者

Nicolet, Y.,Lockridge, O.,Masson, P.,Fontecilla-Camps, J.C.,Nachon, F. (登録日: 2003-04-10, 公開日: 2003-08-05, 最終更新日: 2024-10-16)

主引用文献

Nicolet, Y.,Lockridge, O.,Masson, P.,Fontecilla-Camps, J.C.,Nachon, F.
Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.
J.Biol.Chem., 278:41141-41147, 2003

PubMed Abstract: Cholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave. Human butyrylcholinesterase (BChE) has attracted attention because it can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents. Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding. As expected, the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase. The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected. An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate.

PubMed: 12869558
DOI: 10.1074/jbc.M210241200

実験手法

X-RAY DIFFRACTION (2.3 Å)