2ack

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[[Image:2ack.png|left|200px]]
 
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{{STRUCTURE_2ack| PDB=2ack | SCENE= }}
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==ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, MONOCHROMATIC DATA==
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<StructureSection load='2ack' size='340' side='right'caption='[[2ack]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ack]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetronarce_californica Tetronarce californica]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ack 1ack]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ACK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ACK 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]] 2.4&#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=2ack FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ack OCA], [https://pdbe.org/2ack PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ack RCSB], [https://www.ebi.ac.uk/pdbsum/2ack PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ack 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/ac/2ack_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2ack 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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===ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, MONOCHROMATIC DATA===
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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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{{ABSTRACT_PUBMED_10089512}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2ack" style="background-color:#fffaf0;"></div>
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[[2ack]] is a 1 chain structure of [[Acetylcholinesterase]] with sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ack 1ack]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ACK OCA].
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==See Also==
==See Also==
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*[[AChE inhibitors and substrates|AChE inhibitors and substrates]]
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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*[[AChE inhibitors and substrates (Part II)|AChE inhibitors and substrates (Part II)]]
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== References ==
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*[[AChE inhibitors and substrates (Part III)|AChE inhibitors and substrates (Part III)]]
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<references/>
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*[[Acetylcholinesterase|Acetylcholinesterase]]
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__TOC__
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*[[Journal:Protein Science:1|Journal:Protein Science:1]]
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</StructureSection>
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[[Category: Large Structures]]
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==Reference==
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[[Category: Tetronarce californica]]
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<ref group="xtra">PMID:010089512</ref><ref group="xtra">doi 10.1002/pro.2101</ref><references group="xtra"/>
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[[Category: Harel M]]
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[[Category: Acetylcholinesterase]]
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[[Category: Raves ML]]
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[[Category: Torpedo californica]]
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[[Category: Silman I]]
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[[Category: Harel, M.]]
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[[Category: Sussman JL]]
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[[Category: Raves, M L.]]
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[[Category: Silman, I.]]
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[[Category: Sussman, J L.]]
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[[Category: Carboxylic esterase]]
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[[Category: Hydrolase]]
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Current revision

ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, MONOCHROMATIC DATA

PDB ID 2ack

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