2ACK

ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, MONOCHROMATIC DATA

「1ACK」から置き換えられました

2ACK の概要

• エントリーDOI: 10.2210/pdb2ack/pdb
• 分子名称: ACETYLCHOLINESTERASE, EDROPHONIUM ION (3 entities in total)
• 機能のキーワード: hydrolase, carboxylic esterase
• 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: 60902.76

構造登録者

Raves, M.L.,Sussman, J.L.,Harel, M.,Silman, I. (登録日: 1997-10-29, 公開日: 1998-02-11, 最終更新日: 2024-10-09)

主引用文献

Ravelli, R.B.,Raves, M.L.,Ren, Z.,Bourgeois, D.,Roth, M.,Kroon, J.,Silman, I.,Sussman, J.L.
Static Laue diffraction studies on acetylcholinesterase.
Acta Crystallogr.,Sect.D, 54:1359-1366, 1998

PubMed Abstract: Acetylcholinesterase (AChE) is one of nature's fastest enzymes, despite the fact that its three-dimensional structure reveals its active site to be deeply sequestered within the molecule. This raises questions with respect to traffic of substrate to, and products from, the active site, which may be investigated by time-resolved crystallography. In order to address one aspect of the feasibility of performing time-resolved studies on AChE, a data set has been collected using the Laue technique on a trigonal crystal of Torpedo californica AChE soaked with the reversible inhibitor edrophonium, using a total X-ray exposure time of 24 ms. Electron-density maps obtained from the Laue data, which are of surprisingly good quality compared with similar maps from monochromatic data, show essentially the same features. They clearly reveal the bound ligand, as well as a structural change in the conformation of the active-site Ser200 induced upon binding.

PubMed: 10089512
DOI: 10.1107/S0907444998005277

実験手法

X-RAY DIFFRACTION (2.4 Å)