2c5f

<StructureSection load='2c5f' size='340' side='right'caption='[[2c5f]], [[Resolution|resolution]] 2.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[2c5f]] 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=2C5F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C5F FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHH:N,N,N-TRIMETHYL-4-OXOPENTAN-1-AMINIUM'>CHH</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NWA:4,4-DIHYDROXY-N,N,N-TRIMETHYLPENTAN-1-AMINIUM'>NWA</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c5f OCA], [http://pdbe.org/2c5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c5f RCSB], [http://www.ebi.ac.uk/pdbsum/2c5f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c5f ProSAT]</span></td></tr>

== Function ==

[[http://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.

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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.

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 2c5f" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Acetylcholinesterase]]

[[Category: Colletier, J P]]

[[Category: Fournier, D]]

[[Category: Greenblatt, H M]]

[[Category: Silman, I]]

[[Category: Sussman, J L]]

[[Category: Weik, M]]

[[Category: Zaccai, G]]

[[Category: Synapse]]