1ax9

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{{STRUCTURE_1ax9| PDB=1ax9 | SCENE= }}
 
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===ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, LAUE DATA===
 
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{{ABSTRACT_PUBMED_10089512}}
 
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==About this Structure==
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==ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, LAUE DATA==
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[[1ax9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AX9 OCA].
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<StructureSection load='1ax9' size='340' side='right'caption='[[1ax9]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ax9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetronarce_californica Tetronarce californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AX9 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDR:EDROPHONIUM+ION'>EDR</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ax9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ax9 OCA], [https://pdbe.org/1ax9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ax9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ax9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ax9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACES_TETCF ACES_TETCF] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ax/1ax9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ax9 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==See Also==
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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<ref>PMID:10089512</ref>
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*[[AChE inhibitors and substrates|AChE inhibitors and substrates]]
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*[[AChE inhibitors and substrates (Part II)|AChE inhibitors and substrates (Part II)]]
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*[[Acetylcholinesterase|Acetylcholinesterase]]
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:010089512</ref><references group="xtra"/>
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</div>
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[[Category: Acetylcholinesterase]]
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<div class="pdbe-citations 1ax9" style="background-color:#fffaf0;"></div>
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[[Category: Torpedo californica]]
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[[Category: Harel, M.]]
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==See Also==
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[[Category: Ravelli, R B.G.]]
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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[[Category: Raves, M L.]]
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== References ==
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[[Category: Silman, I.]]
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<references/>
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[[Category: Sussman, J L.]]
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__TOC__
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[[Category: Carboxylic esterase]]
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</StructureSection>
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[[Category: Hydrolase]]
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[[Category: Large Structures]]
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[[Category: Serine esterase]]
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[[Category: Tetronarce californica]]
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[[Category: Synapse]]
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[[Category: Harel M]]
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[[Category: Ravelli RBG]]
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[[Category: Raves ML]]
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[[Category: Silman I]]
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[[Category: Sussman JL]]

Current revision

ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, LAUE DATA

PDB ID 1ax9

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