View source for 2vt6


==Native Torpedo californica acetylcholinesterase collected with a cumulated dose of 9400000 Gy==
<StructureSection load='2vt6' size='340' side='right'caption='[[2vt6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vt6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VT6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zgb|1zgb]], [[1qti|1qti]], [[1amn|1amn]], [[1e66|1e66]], [[2vq6|2vq6]], [[2j3d|2j3d]], [[2ack|2ack]], [[1qii|1qii]], [[2ckm|2ckm]], [[1dx6|1dx6]], [[1qij|1qij]], [[1qie|1qie]], [[1acl|1acl]], [[1w4l|1w4l]], [[1odc|1odc]], [[2cmf|2cmf]], [[2j3q|2j3q]], [[1gqs|1gqs]], [[2j4f|2j4f]], [[1e3q|1e3q]], [[2dfp|2dfp]], [[1qik|1qik]], [[2c5f|2c5f]], [[1ea5|1ea5]], [[2vjc|2vjc]], [[1eea|1eea]], [[1qif|1qif]], [[2vjb|2vjb]], [[1qig|1qig]], [[1zgc|1zgc]], [[1qid|1qid]], [[2vjd|2vjd]], [[1jjb|1jjb]], [[1ut6|1ut6]], [[2vt7|2vt7]], [[2cek|2cek]], [[1qim|1qim]], [[1gpk|1gpk]], [[1jga|1jga]], [[3ace|3ace]], [[1oce|1oce]], [[1w6r|1w6r]], [[1som|1som]], [[1vxo|1vxo]], [[2vja|2vja]], [[1cfj|1cfj]], [[2v96|2v96]], [[1ax9|1ax9]], [[1u65|1u65]], [[1w76|1w76]], [[1h22|1h22]], [[1eve|1eve]], [[2c4h|2c4h]], [[1gqr|1gqr]], [[2ace|2ace]], [[2va9|2va9]], [[1vxr|1vxr]], [[4ace|4ace]], [[2c58|2c58]], [[1hbj|1hbj]], [[1vot|1vot]], [[1w75|1w75]], [[2c5g|2c5g]], [[1jgb|1jgb]], [[2v98|2v98]], [[1gpn|1gpn]], [[1qih|1qih]], [[1h23|1h23]], [[1acj|1acj]], [[1fss|1fss]], [[2v97|2v97]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vt6 OCA], [https://pdbe.org/2vt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vt6 RCSB], [https://www.ebi.ac.uk/pdbsum/2vt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vt6 ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/ACES_TORCA ACES_TORCA]] 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. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vt/2vt6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2vt6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Although x-ray crystallography is the most widely used method for macromolecular structure determination, it does not provide dynamical information, and either experimental tricks or complementary experiments must be used to overcome the inherently static nature of crystallographic structures. Here we used specific x-ray damage during temperature-controlled crystallographic experiments at a third-generation synchrotron source to trigger and monitor (Shoot-and-Trap) structural changes putatively involved in an enzymatic reaction. In particular, a nonhydrolyzable substrate analogue of acetylcholinesterase, the "off-switch" at cholinergic synapses, was radiocleaved within the buried enzymatic active site. Subsequent product clearance, observed at 150 K but not at 100 K, indicated exit from the active site possibly via a "backdoor." The simple strategy described here is, in principle, applicable to any enzyme whose structure in complex with a substrate analogue is available and, therefore, could serve as a standard procedure in kinetic crystallography studies.

Shoot-and-Trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography.,Colletier JP, Bourgeois D, Sanson B, Fournier D, Sussman JL, Silman I, Weik M Proc Natl Acad Sci U S A. 2008 Aug 19;105(33):11742-7. Epub 2008 Aug 13. PMID:18701720<ref>PMID:18701720</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2vt6" style="background-color:#fffaf0;"></div>

==See Also==
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acetylcholinesterase]]
[[Category: Large Structures]]
[[Category: Torpedo californica]]
[[Category: Bourgeois, D]]
[[Category: Colletier, J P]]
[[Category: Fournier, D]]
[[Category: Sanson, B]]
[[Category: Silman, I]]
[[Category: Sussman, J L]]
[[Category: Weik, M]]
[[Category: Alternative splicing]]
[[Category: Cell junction]]
[[Category: Glycoprotein]]
[[Category: Gpi-anchor]]
[[Category: Hydrolase]]
[[Category: Lipoprotein]]
[[Category: Membrane]]
[[Category: Native torpedo californica acetylcholinesterase]]
[[Category: Neurotransmitter degradation]]
[[Category: Serine esterase]]
[[Category: Synapse]]