2ack | pdb_00002ack

ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, MONOCHROMATIC DATA

spinqualitylabelsall models 2ack, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ack is a 1 chain structure with sequence from Torpedo californica. This structure supersedes the now removed PDB entry 1ack. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDR Activity: Acetylcholinesterase, with EC number 3.1.1.7 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Static Laue diffraction studies on acetylcholinesterase.,Ravelli RB, Raves ML, Ren Z, Bourgeois D, Roth M, Kroon J, Silman I, Sussman JL Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1359-66. PMID:10089512 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also AChE inhibitors and substrates AChE inhibitors and substrates (Part II) AChE inhibitors and substrates (Part III) Acetylcholinesterase Journal:Protein Science:1

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