2c5g: Difference between revisions

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[[Image:2c5g.png|left|200px]]


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==Torpedo californica acetylcholinesterase in complex with 20mM thiocholine==
The line below this paragraph, containing "STRUCTURE_2c5g", creates the "Structure Box" on the page.
<StructureSection load='2c5g' size='340' side='right'caption='[[2c5g]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
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<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>
{{STRUCTURE_2c5g|  PDB=2c5g  |  SCENE=  }}
<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].
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== 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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2c5g" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_16763558}}, adds the Publication Abstract to the page
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 16763558 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_16763558}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2C5G is a 1 chain structure of 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].
[[Category: Colletier JP]]
 
[[Category: Fournier D]]
==Reference==
[[Category: Greenblatt HM]]
<ref group="xtra">PMID:16763558</ref><references group="xtra"/>
[[Category: Silman I]]
[[Category: Acetylcholinesterase]]
[[Category: Sussman JL]]
[[Category: Torpedo californica]]
[[Category: Weik M]]
[[Category: Colletier, J P.]]
[[Category: Zaccai G]]
[[Category: Fournier, D.]]
[[Category: Greenblatt, H M.]]
[[Category: Silman, I.]]
[[Category: Sussman, J L.]]
[[Category: Weik, M.]]
[[Category: Zaccai, G.]]
[[Category: Alpha/beta hydrolase]]
[[Category: Alternative splicing]]
[[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]]
 
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