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1f8u

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CRYSTAL STRUCTURE OF MUTANT E202Q OF HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH GREEN MAMBA VENOM PEPTIDE FASCICULIN-II

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-[[Image:1f8u.gif|left|200px]]<br />
-<applet load="1f8u" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1f8u, resolution 2.90&Aring;" />
-'''CRYSTAL STRUCTURE OF MUTANT E202Q OF HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH GREEN MAMBA VENOM PEPTIDE FASCICULIN-II'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF MUTANT E202Q OF HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH GREEN MAMBA VENOM PEPTIDE FASCICULIN-II==
-Structures of recombinant wild-type human acetylcholinesterase and of its, E202Q mutant as complexes with fasciculin-II, a 'three-finger' polypeptide, toxin purified from the venom of the eastern green mamba (Dendroaspis, angusticeps), are reported. The structure of the complex of the wild-type, enzyme was solved to 2.8 A resolution by molecular replacement starting, from the structure of the complex of Torpedo californica, acetylcholinesterase with fasciculin-II and verified by starting from a, similar complex with mouse acetylcholinesterase. The overall structure is, surprisingly similar to that of the T. californica enzyme with, fasciculin-II and, as expected, to that of the mouse acetylcholinesterase, complex. The structure of the E202Q mutant complex was refined starting, from the corresponding wild-type human acetylcholinesterase structure, using the 2.7 A resolution data set collected. Comparison of the two, structures shows that removal of the charged group from the protein core, and its substitution by a neutral isosteric moiety does not disrupt the, functional architecture of the active centre. One of the elements of this, architecture is thought to be a hydrogen-bond network including residues, Glu202, Glu450, Tyr133 and two bridging molecules of water, which is, conserved in other vertebrate acetylcholinesterases as well as in the, human enzyme. The present findings are consistent with the notion that the, main role of this network is the proper positioning of the Glu202, carboxylate relative to the catalytic triad, thus defining its functional, role in the interaction of acetylcholinesterase with substrates and, inhibitors.
+<StructureSection load='1f8u' size='340' side='right'caption='[[1f8u]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1f8u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F8U FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f8u OCA], [https://pdbe.org/1f8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f8u RCSB], [https://www.ebi.ac.uk/pdbsum/1f8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f8u ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref> <ref>PMID:1748670</ref> <ref>PMID:1517212</ref> <ref>PMID:11985878</ref>
+== 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/f8/1f8u_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=1f8u ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-F8U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F8U OCA].
+*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
+*[[Fasciculin|Fasciculin]]
-==Reference==
+== References ==
-Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II., Kryger G, Harel M, Giles K, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL, Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1385-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11053835 11053835]
+<references/>
-[[Category: Acetylcholinesterase]]
+__TOC__
+</StructureSection>
 [[Category: Dendroaspis angusticeps]]
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Harel, M.]]
+[[Category: Harel M]]
-[[Category: Kryger, G.]]
+[[Category: Kryger G]]
-[[Category: Shafferman, A.]]
+[[Category: Shafferman A]]
-[[Category: Silman, I.]]
+[[Category: Silman I]]
-[[Category: Sussman, J.L.]]
+[[Category: Sussman JL]]
-[[Category: human acetylcholinesterase]]
-[[Category: hydrolase]]
-[[Category: hydrolase/hydrolase inhibitor]]
-[[Category: serine esterase]]
-[[Category: snake toxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov  8 12:40:03 2007''

1f8u

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CRYSTAL STRUCTURE OF MUTANT E202Q OF HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH GREEN MAMBA VENOM PEPTIDE FASCICULIN-II

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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