2ace
From Proteopedia
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| - | + | ==NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA== | |
| - | + | <StructureSection load='2ace_au' size='340' side='right' caption='[[2ace]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2ace]] is a 1 chain structure with sequence from [http://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=1ace 1ace]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ACE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ACE FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACH:ACETYLCHOLINE'>ACH</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ace FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ace OCA], [http://pdbe.org/2ace PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ace RCSB], [http://www.ebi.ac.uk/pdbsum/2ace PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ace ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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. | ||
| + | == 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/ac/2ace_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=2ace ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | (-)-Huperzine A (HupA) is found in an extract from a club moss that has been used for centuries in Chinese folk medicine. Its action has been attributed to its ability to strongly inhibit acetylcholinesterase (AChE). The crystal structure of the complex of AChE with optically pure HupA at 2.5 A resolution shows an unexpected orientation for the inhibitor with surprisingly few strong direct interactions with protein residues to explain its high affinity. This structure is compared to the native structure of AChE devoid of any inhibitor as determined to the same resolution. An analysis of the affinities of structural analogues of HupA, correlated with their interactions with the protein, shows the importance of individual hydrophobic interactions between HupA and aromatic residues in the active-site gorge of AChE. | ||
| - | + | Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.,Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL Nat Struct Biol. 1997 Jan;4(1):57-63. PMID:8989325<ref>PMID:8989325</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2ace" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[AChE bivalent inhibitors|AChE bivalent inhibitors]] | ||
*[[AChE inhibitors and substrates|AChE inhibitors and substrates]] | *[[AChE inhibitors and substrates|AChE inhibitors and substrates]] | ||
| - | *[[AChE inhibitors and substrates (Part III)|AChE inhibitors and substrates (Part III)]] | ||
*[[Acetylcholine|Acetylcholine]] | *[[Acetylcholine|Acetylcholine]] | ||
*[[Acetylcholinesterase|Acetylcholinesterase]] | *[[Acetylcholinesterase|Acetylcholinesterase]] | ||
*[[Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane|Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane]] | *[[Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane|Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane]] | ||
*[[Acetylcholinesterase with DFP|Acetylcholinesterase with DFP]] | *[[Acetylcholinesterase with DFP|Acetylcholinesterase with DFP]] | ||
| + | *[[Acetylcholinesterase: Substrate Traffic and Inhibition|Acetylcholinesterase: Substrate Traffic and Inhibition]] | ||
| + | *[[Ejemplo1acj|Ejemplo1acj]] | ||
*[[Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)|Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)]] | *[[Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)|Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)]] | ||
*[[Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)|Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)]] | *[[Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)|Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)]] | ||
| - | + | *[[3D structures of acetylcholinesterase|3D structures of acetylcholinesterase]] | |
| - | == | + | == References == |
| - | < | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Acetylcholinesterase]] | [[Category: Acetylcholinesterase]] | ||
| - | [[Category: | + | [[Category: Tetronarce californica]] |
| - | [[Category: Harel, M | + | [[Category: Harel, M]] |
| - | [[Category: Raves, M L | + | [[Category: Raves, M L]] |
| - | [[Category: Silman, I | + | [[Category: Silman, I]] |
| - | [[Category: Sussman, J L | + | [[Category: Sussman, J L]] |
[[Category: Alpha/beta hydrolase]] | [[Category: Alpha/beta hydrolase]] | ||
[[Category: Catalytic triad]] | [[Category: Catalytic triad]] | ||
[[Category: Neurotransmitter cleavage]] | [[Category: Neurotransmitter cleavage]] | ||
[[Category: Serine hydrolase]] | [[Category: Serine hydrolase]] | ||
Current revision
NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA
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