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<StructureSection load='ACHE2.pdb' size='400' side='right' scene='2ace/Com_view/1' caption=''> [[Image:2ace.jpg|left|200px]]<br /> <!-- The below STRUCTURE_2ace Template creates the "Structure Box" on the page. You may change the PDB parameter (setting the PDB file loaded) or the SCENE parameter (setting the initial scene to display when the page is loaded), or leave the SCENE parameter empty for the default display. --> '''ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM ''TORPEDO CALIFORNICA''''' (see also [[AChE inhibitors and substrates]]) {{ABSTRACT_PUBMED_8989325}} {{Clear}} ==Overview== Solution of the three-dimensional (3D) structure of [http://en.wikipedia.org/wiki/Pacific_electric_ray ''Torpedo californica''] [[acetylcholinesterase]] (''Tc''AChE) in 1991 ([http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1678899 Sussman ''et al''. & Silman (1991)]) opened up new horizons in research on an [http://en.wikipedia.org/wiki/Enzyme enzyme] that had already been the subject of intensive investigation. The unanticipated structure of this extremely rapid enzyme, in which the active site was found to be buried at the bottom of a <scene name='2ace/Active_site/3'>deep and narrow gorge</scene>, lined by <scene name='2ace/Active_site/4'>14 aromatic residues</scene> <font color='darkmagenta'><b>(colored darkmagenta)</b></font>, led to a revision of the views then held concerning substrate traffic, recognition, and hydrolysis ([http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10545346 Botti ''et al''. Sussman & Silman (1999)]). This led to a series of theoretical and experimental studies, which took advantage of recent advances in theoretical techniques for treatment of [http://en.wikipedia.org/wiki/Protein proteins], such as [http://en.wikipedia.org/wiki/Molecular_dynamics molecular dynamics] and [http://en.wikipedia.org/wiki/Electrostatics electrostatics] and to [http://en.wikipedia.org/wiki/Site-directed_mutagenesis site-directed mutagenesis], utilizing suitable expression systems. [http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase] [http://en.wikipedia.org/wiki/Hydrolysis hydrolysizes] the [http://en.wikipedia.org/wiki/Neurotransmitter neurotransmitter] [http://en.wikipedia.org/wiki/Acetylcholine acetylcholine] <scene name='2ace/Cv/2'>(ACh)</scene>, producing <scene name='2ace/Cv/3'>choline and an acetate</scene> group. ACh directly binds <scene name='2ace/Cv/4'>Ser200</scene> (via its [http://en.wikipedia.org/wiki/Nucleophile nucleophilic] Oγ atom) within the <scene name='2ace/Cv/5'>catalytic triad (Ser200, His440, and Glu327)</scene>. The residues <scene name='2ace/Cv/6'>Trp84 and Phe330</scene> are also important in the [http://en.wikipedia.org/wiki/Ligand ligand] recognition. After this binding acetylcholinesterase <scene name='2ace/Cv/7'>hydrolysizes</scene> ACh. ==About this Structure== 2ACE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica] with ACH as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1ACE. Active as [[Acetylcholinesterase]], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] Structure known Active Site: CAT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ACE OCA]. ===Additional Resources=== For additional information, see: [[Alzheimer's Disease]] </StructureSection> ==Reference== 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8989325 8989325] [[Category: Acetylcholinesterase]] [[Category: Single protein]] [[Category: Torpedo californica]] [[Category: Harel, M.]] [[Category: Raves, M.L.]] [[Category: Silman, I.]] [[Category: Sussman, J.L.]] [[Category: ACH]] [[Category: alpha/beta hydrolase]] [[Category: catalytic triad]] [[Category: neurotransmitter cleavage]] [[Category: serine hydrolase]] <br /> *Created with the participation of [[User:Joel L. Sussman|Joel L. Sussman]], [[User:Jaime Prilusky|Jaime Prilusky]], [[User:David Canner|David Canner]].

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