1mz6: Difference between revisions
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== Structural highlights == | == 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 [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> | ||
</td></tr><tr><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><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> | ||
<tr><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='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><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='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><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> | <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> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Exo-alpha-sialidase]] | [[Category: Exo-alpha-sialidase]] | ||
[[Category: Trypanosoma rangeli]] | [[Category: Trypanosoma rangeli]] | ||
[[Category: Alzari, P M | [[Category: Alzari, P M]] | ||
[[Category: Amaya, M F | [[Category: Amaya, M F]] | ||
[[Category: Buschiazzo, A | [[Category: Buschiazzo, A]] | ||
[[Category: Campetella, O | [[Category: Campetella, O]] | ||
[[Category: Cremona, M L | [[Category: Cremona, M L]] | ||
[[Category: Frasch, A C.C | [[Category: Frasch, A C.C]] | ||
[[Category: Paris, G | [[Category: Paris, G]] | ||
[[Category: Spinelli, S | [[Category: Spinelli, S]] | ||
[[Category: Tavares, G A | [[Category: Tavares, G A]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Hydrolase inhibitor]] | [[Category: Hydrolase inhibitor]] | ||
Revision as of 19:02, 5 January 2015
Trypanosoma rangeli sialidase in complex with the inhibitor DANATrypanosoma rangeli sialidase in complex with the inhibitor DANA
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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