2c5g: Difference between revisions

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-[[Image:2c5g.png|left|200px]]
-{{STRUCTURE_2c5g|  PDB=2c5g  |  SCENE=  }}
+==Torpedo californica acetylcholinesterase in complex with 20mM thiocholine==
+<StructureSection load='2c5g' size='340' side='right'caption='[[2c5g]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C5G FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</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=ETM:2-(TRIMETHYLAMMONIUM)ETHYL+THIOL'>ETM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></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=2c5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c5g OCA], [https://pdbe.org/2c5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c5g RCSB], [https://www.ebi.ac.uk/pdbsum/2c5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c5g ProSAT]</span></td></tr>
+</table>
+== 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/c5/2c5g_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2c5g ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Acetylcholinesterase (AChE) terminates nerve-impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter, acetylcholine. Substrate traffic in AChE involves at least two binding sites, the catalytic and peripheral anionic sites, which have been suggested to be allosterically related and involved in substrate inhibition. Here, we present the crystal structures of Torpedo californica AChE complexed with the substrate acetylthiocholine, the product thiocholine and a nonhydrolysable substrate analogue. These structures provide a series of static snapshots of the substrate en route to the active site and identify, for the first time, binding of substrate and product at both the peripheral and active sites. Furthermore, they provide structural insight into substrate inhibition in AChE at two different substrate concentrations. Our structural data indicate that substrate inhibition at moderate substrate concentration is due to choline exit being hindered by a substrate molecule bound at the peripheral site. At the higher concentration, substrate inhibition arises from prevention of exit of acetate due to binding of two substrate molecules within the active-site gorge.
-===TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH 20MM THIOCHOLINE===
+Structural insights into substrate traffic and inhibition in acetylcholinesterase.,Colletier JP, Fournier D, Greenblatt HM, Stojan J, Sussman JL, Zaccai G, Silman I, Weik M EMBO J. 2006 Jun 21;25(12):2746-56. Epub 2006 Jun 8. PMID:16763558<ref>PMID:16763558</ref>
-{{ABSTRACT_PUBMED_16763558}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2c5g" style="background-color:#fffaf0;"></div>
-[[2c5g]] is a 1 chain structure of [[Acetylcholinesterase]] 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=2C5G OCA].
 ==See Also==
-*[[Acetylcholinesterase|Acetylcholinesterase]]
+*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:016763558</ref><references group="xtra"/>
+__TOC__
-[[Category: Acetylcholinesterase]]
+</StructureSection>
-[[Category: Torpedo californica]]
+[[Category: Large Structures]]
-[[Category: Colletier, J P.]]
+[[Category: Colletier JP]]
-[[Category: Fournier, D.]]
+[[Category: Fournier D]]
-[[Category: Greenblatt, H M.]]
+[[Category: Greenblatt HM]]
-[[Category: Silman, I.]]
+[[Category: Silman I]]
-[[Category: Sussman, J L.]]
+[[Category: Sussman JL]]
-[[Category: Weik, M.]]
+[[Category: Weik M]]
-[[Category: Zaccai, G.]]
+[[Category: Zaccai G]]
-[[Category: Alpha/beta hydrolase]]
-[[Category: Anchor]]
-[[Category: Glycoprotein]]
-[[Category: Hydrolase]]
-[[Category: Lipoprotein]]
-[[Category: Membrane]]
-[[Category: Michaelis-menten complex]]
-[[Category: Neurotransmitter cleavage]]
-[[Category: Serine esterase]]
-[[Category: Substrate hydrolysis]]
-[[Category: Substrate inhibition]]
-[[Category: Synapse]]