1mz6: Difference between revisions

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OCA

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 ==Trypanosoma rangeli sialidase in complex with the inhibitor DANA==
-<StructureSection load='1mz6' size='340' side='right' caption='[[1mz6]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='1mz6' size='340' side='right'caption='[[1mz6]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mz6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trypanosoma_rangeli Trypanosoma rangeli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MZ6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mz6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_rangeli Trypanosoma rangeli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZ6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mz5|1mz5]], [[1mr5|1mr5]], [[1ms0|1ms0]], [[1ms1|1ms1]], [[1ms3|1ms3]], [[1ms4|1ms4]], [[1ms5|1ms5]], [[1ms8|1ms8]], [[1ms9|1ms9]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></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=1mz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mz6 OCA], [https://pdbe.org/1mz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mz6 RCSB], [https://www.ebi.ac.uk/pdbsum/1mz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mz6 ProSAT]</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=1mz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mz6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mz6 RCSB], [http://www.ebi.ac.uk/pdbsum/1mz6 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/O44049_TRYRA O44049_TRYRA]
 == 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/mz/1mz6_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/1mz6_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1mz6 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The intracellular parasite Trypanosoma cruzi, the etiological agent of Chagas disease, sheds a developmentally regulated surface trans-sialidase, which is involved in key aspects of parasite-host cell interactions. Although it shares a common active site architecture with bacterial neuraminidases, the T.cruzi enzyme behaves as a highly efficient sialyltransferase. Here we report the crystal structure of the closely related Trypanosoma rangeli sialidase and its complex with inhibitor. The enzyme folds into two distinct domains: a catalytic beta-propeller fold tightly associated with a lectin-like domain. Comparison with the modeled structure of T.cruzi trans-sialidase and mutagenesis experiments allowed the identification of amino acid substitutions within the active site cleft that modulate sialyltransferase activity and suggest the presence of a distinct binding site for the acceptor carbohydrate. The structures of the Trypanosoma enzymes illustrate how a glycosidase scaffold can achieve efficient glycosyltransferase activity and provide a framework for structure-based drug design.
-Structural basis of sialyltransferase activity in trypanosomal sialidases.,Buschiazzo A, Tavares GA, Campetella O, Spinelli S, Cremona ML, Paris G, Amaya MF, Frasch AC, Alzari PM EMBO J. 2000 Jan 4;19(1):16-24. PMID:10619840<ref>PMID:10619840</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Exo-alpha-sialidase]]
+[[Category: Large Structures]]
 [[Category: Trypanosoma rangeli]]
-[[Category: Alzari, P M]]
+[[Category: Alzari PM]]
-[[Category: Amaya, M F]]
+[[Category: Amaya MF]]
-[[Category: Buschiazzo, A]]
+[[Category: Buschiazzo A]]
-[[Category: Campetella, O]]
+[[Category: Campetella O]]
-[[Category: Cremona, M L]]
+[[Category: Cremona ML]]
-[[Category: Frasch, A C.C]]
+[[Category: Frasch ACC]]
-[[Category: Paris, G]]
+[[Category: Paris G]]
-[[Category: Spinelli, S]]
+[[Category: Spinelli S]]
-[[Category: Tavares, G A]]
+[[Category: Tavares GA]]
-[[Category: Hydrolase]]
-[[Category: Hydrolase inhibitor]]
-[[Category: Inibitor complex]]
-[[Category: Sialyltransferase]]
-[[Category: Trypanosomal sialidase]]