Ravelli_1998_Acta.Crystallogr.D.Biol.Crystallogr_54_1359

Reference

Title : Static laue diffraction studies on acetylcholinesterase - Ravelli_1998_Acta.Crystallogr.D.Biol.Crystallogr_54_1359
Author(s) : Ravelli RB , Raves ML , Ren Z , Bourgeois D , Roth M , Kroon J , Silman I , Sussman JL
Ref : Acta Crystallographica D Biol Crystallogr , 54 :1359 , 1998
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.

PubMedSearch : Ravelli_1998_Acta.Crystallogr.D.Biol.Crystallogr_54_1359
PubMedID: 10089512
Gene_locus related to this paper: torca-ACHE

Related information

Inhibitor Edrophonium
Gene_locus Edrophonium    torca-ACHE
Structure Edrophonium    torca-ACHE    1AX9

Citations formats

Ravelli RB, Raves ML, Ren Z, Bourgeois D, Roth M, Kroon J, Silman I, Sussman JL (1998)
Static laue diffraction studies on acetylcholinesterase
Acta Crystallographica D Biol Crystallogr 54 :1359

Ravelli RB, Raves ML, Ren Z, Bourgeois D, Roth M, Kroon J, Silman I, Sussman JL (1998)
Acta Crystallographica D Biol Crystallogr 54 :1359