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1mz5
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mz5]] 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=1MZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZ5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1mz5]] 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=1MZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZ5 FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id=' | + | <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> |
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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=1mz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mz5 OCA], [https://pdbe.org/1mz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mz5 RCSB], [https://www.ebi.ac.uk/pdbsum/1mz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mz5 ProSAT]</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=1mz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mz5 OCA], [https://pdbe.org/1mz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mz5 RCSB], [https://www.ebi.ac.uk/pdbsum/1mz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mz5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O44049_TRYRA O44049_TRYRA] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1mz5 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=1mz5 ConSurf]. | ||
<div style="clear:both"></div> | <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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1mz5" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Exo-alpha-sialidase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Trypanosoma rangeli]] | [[Category: Trypanosoma rangeli]] | ||
| - | [[Category: Alzari | + | [[Category: Alzari PM]] |
| - | [[Category: Amaya | + | [[Category: Amaya MF]] |
| - | [[Category: Buschiazzo | + | [[Category: Buschiazzo A]] |
| - | [[Category: Campetella | + | [[Category: Campetella O]] |
| - | [[Category: Cremona | + | [[Category: Cremona ML]] |
| - | [[Category: Frasch | + | [[Category: Frasch ACC]] |
| - | [[Category: Paris | + | [[Category: Paris G]] |
| - | [[Category: Spinelli | + | [[Category: Spinelli S]] |
| - | [[Category: Tavares | + | [[Category: Tavares GA]] |
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Current revision
Trypanosoma rangeli sialidase
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