2j3q: Difference between revisions

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-[[Image:2j3q.png|left|200px]]
-<!--
+==Torpedo acetylcholinesterase complexed with fluorophore thioflavin T==
-The line below this paragraph, containing "STRUCTURE_2j3q", creates the "Structure Box" on the page.
+<StructureSection load='2j3q' size='340' side='right'caption='[[2j3q]], [[Resolution|resolution]] 2.80&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'>[[2j3q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetronarce_californica Tetronarce californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J3Q 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]] 2.8&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TFL:2-[4-(DIMETHYLAMINO)PHENYL]-6-HYDROXY-3-METHYL-1,3-BENZOTHIAZOL-3-IUM'>TFL</scene></td></tr>
-{{STRUCTURE_2j3q|  PDB=2j3q  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j3q OCA], [https://pdbe.org/2j3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j3q RCSB], [https://www.ebi.ac.uk/pdbsum/2j3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j3q ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACES_TETCF ACES_TETCF] 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/j3/2j3q_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=2j3q ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Acetylcholinesterase plays a key role in cholinergic synaptic transmission by hydrolyzing the neurotransmitter acetylcholine with one of the highest known catalytic rate constants. Hydrolysis occurs in a narrow and deep gorge that contains two sites of ligand binding: A peripheral site, or P-site, near the gorge entrance that contributes to catalytic efficiency both by transiently trapping substrate molecules as they enter the gorge and by allosterically accelerating the transfer of the substrate acyl group to a serine hydroxyl in an acylation site or A-site at the base of the gorge. Thioflavin T is a useful reporter of ligand interactions with the A-site. It binds specifically to the P-site with fluorescence that is enhanced approximately 1000-fold over that of unbound thioflavin T, and the enhanced fluorescence is quenched 1.5- to 4-fold when another ligand binds to the A-site in a ternary complex. To clarify the structural basis of this advantageous signal change, we here report the X-ray structure of the complex of thioflavin T with Torpedo californica acetylcholinesterase. The two aromatic rings in thioflavin T are coplanar and are packed snugly parallel to the aromatic side chains of Trp279, Tyr334, and Phe330. Overlays of this structure with the crystal structures of Torpedo californica acetylcholinesterase complexes with either edrophonium or m-( N, N, N-trimethylammonio)-2,2,2-trifluoroacetophenone, two small aromatic ligands that bind specifically to the A-site, indicate that the phenyl side chain of Phe330 must rotate to sterically accommodate both thioflavin T and the A-site ligand in the ternary complex. This rotation may allow some relaxation of the strict coplanarity of the aromatic rings in the bound thioflavin T and result in partial quenching of its fluorescence.
-===TORPEDO ACETYLCHOLINESTERASE COMPLEXED WITH FLUOROPHORE THIOFLAVIN T===
+Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site.,Harel M, Sonoda LK, Silman I, Sussman JL, Rosenberry TL J Am Chem Soc. 2008 Jun 25;130(25):7856-61. Epub 2008 May 31. PMID:18512913<ref>PMID:18512913</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_18512913}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2j3q" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 18512913 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_18512913}}
-==About this Structure==
-[[2j3q]] is a 1 chain structure of [[Acetylcholinesterase]] 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=2J3Q OCA].
 ==See Also==
-*[[AChE inhibitors and substrates (Part III)|AChE inhibitors and substrates (Part III)]]
+*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
-*[[Acetylcholinesterase|Acetylcholinesterase]]
+== References ==
-*[[Alzheimer's Disease|Alzheimer's Disease]]
+<references/>
+__TOC__
-==Reference==
+</StructureSection>
-<ref group="xtra">PMID:018512913</ref><references group="xtra"/>
+[[Category: Large Structures]]
-[[Category: Acetylcholinesterase]]
+[[Category: Tetronarce californica]]
-[[Category: Torpedo californica]]
+[[Category: Cusack B]]
-[[Category: Cusack, B.]]
+[[Category: Harel M]]
-[[Category: Harel, M.]]
+[[Category: Johnson JL]]
-[[Category: Johnson, J L.]]
+[[Category: Rosenberry TL]]
-[[Category: Rosenberry, T L.]]
+[[Category: Silman I]]
-[[Category: Silman, I.]]
+[[Category: Sussman JL]]
-[[Category: Sussman, J L.]]
-[[Category: Anticancer prodrug cpt- 11]]
-[[Category: Glycoprotein]]
-[[Category: Gpi-anchor]]
-[[Category: Hydrolase]]
-[[Category: Lipoprotein]]
-[[Category: Membrane]]
-[[Category: Neurotransmitter degradation]]
-[[Category: Serine esterase]]
-[[Category: Synapse]]
-[[Category: Torpedo ache]]