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| - | | + | #REDIRECT [[6xyy]] This PDB entry is obsolete and replaced by 6xyy |
| - | ==ACHE FROM DROSOPHILA MELANOGASTER COMPLEX WITH TACRINE DERIVATIVE 9-(3-PHENYLMETHYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE==
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| - | <StructureSection load='1dx4' size='340' side='right'caption='[[1dx4]], [[Resolution|resolution]] 2.70Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[1dx4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DX4 FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=760:9-(3-PHENYLMETHYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE'>760</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dx4 OCA], [https://pdbe.org/1dx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dx4 RCSB], [https://www.ebi.ac.uk/pdbsum/1dx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dx4 ProSAT]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[https://www.uniprot.org/uniprot/ACES_DROME ACES_DROME]] Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine.
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| - | == Evolutionary Conservation ==
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| - | [[Image:Consurf_key_small.gif|200px|right]]
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| - | Check<jmol>
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| - | <jmolCheckbox>
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| - | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dx/1dx4_consurf.spt"</scriptWhenChecked>
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| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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| - | <text>to colour the structure by Evolutionary Conservation</text>
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| - | </jmolCheckbox>
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| - | </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=1dx4 ConSurf].
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| - | <div style="clear:both"></div>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | We have crystallized Drosophila melanogaster acetylcholinesterase and solved the structure of the native enzyme and of its complexes with two potent reversible inhibitors, 1,2,3,4-tetrahydro-N-(phenylmethyl)-9-acridinamine and 1,2,3,4-tetrahydro-N-(3-iodophenyl-methyl)-9-acridinamine--all three at 2.7 A resolution. The refined structure of D. melanogaster acetylcholinesterase is similar to that of vertebrate acetylcholinesterases, for example, human, mouse, and fish, in its overall fold, charge distribution, and deep active-site gorge, but some of the surface loops deviate by up to 8 A from their position in the vertebrate structures, and the C-terminal helix is shifted substantially. The active-site gorge of the insect enzyme is significantly narrower than that of Torpedo californica AChE, and its trajectory is shifted several angstroms. The volume of the lower part of the gorge of the insect enzyme is approximately 50% of that of the vertebrate enzyme. Upon binding of either of the two inhibitors, nine aromatic side chains within the active-site gorge change their conformation so as to interact with the inhibitors. Some differences in activity and specificity between the insect and vertebrate enzymes can be explained by comparison of their three-dimensional structures.
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| - | Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors.,Harel M, Kryger G, Rosenberry TL, Mallender WD, Lewis T, Fletcher RJ, Guss JM, Silman I, Sussman JL Protein Sci. 2000 Jun;9(6):1063-72. PMID:10892800<ref>PMID:10892800</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 1dx4" style="background-color:#fffaf0;"></div>
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| - | ==See Also==
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| - | *[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Acetylcholinesterase]]
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| - | [[Category: Drome]]
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| - | [[Category: Large Structures]]
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| - | [[Category: Harel, M]]
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| - | [[Category: Silman, I]]
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| - | [[Category: Sussman, J L]]
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| - | [[Category: Glycoprotein]]
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| - | [[Category: Gpi-anchor]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Membrane]]
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| - | [[Category: Muscle]]
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| - | [[Category: Nerve]]
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| - | [[Category: Neurotransmitter degradation]]
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| - | [[Category: Serine esterase]]
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| - | [[Category: Synapse]]
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