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| | <StructureSection load='3pjq' size='340' side='right'caption='[[3pjq]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='3pjq' size='340' side='right'caption='[[3pjq]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pjq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trycr Trycr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PJQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pjq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_cruzi Trypanosoma cruzi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PJQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1s0i|1s0i]], [[1s0j|1s0j]], [[1ms0|1ms0]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900008:alpha-lactose'>PRD_900008</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></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=3pjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pjq OCA], [https://pdbe.org/3pjq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pjq RCSB], [https://www.ebi.ac.uk/pdbsum/3pjq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pjq 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=3pjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pjq OCA], [https://pdbe.org/3pjq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pjq RCSB], [https://www.ebi.ac.uk/pdbsum/3pjq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pjq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q26966_TRYCR Q26966_TRYCR] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Exo-alpha-sialidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trycr]] | + | [[Category: Trypanosoma cruzi]] |
| - | [[Category: Alzari, P M]] | + | [[Category: Alzari PM]] |
| - | [[Category: Baraibar, M]] | + | [[Category: Baraibar M]] |
| - | [[Category: Buschiazzo, A]] | + | [[Category: Buschiazzo A]] |
| - | [[Category: Obal, G]] | + | [[Category: Obal G]] |
| - | [[Category: Oppezzo, P]] | + | [[Category: Oppezzo P]] |
| - | [[Category: Pritsch, O]] | + | [[Category: Pritsch O]] |
| - | [[Category: Beta-propeller]]
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| - | [[Category: Lactose]]
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| - | [[Category: Lectin / similar to actve trans-sialidase]]
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| - | [[Category: Sugar binding protein]]
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| Structural highlights
Function
Q26966_TRYCR
Publication Abstract from PubMed
Trans-sialidases are surface-located proteins in Trypanosoma cruzi that participate in key parasite-host interactions and parasite virulence. These proteins are encoded by a large multigenic family, with tandem-repeated and individual genes dispersed throughout the genome. While a large number of genes encode for catalytically active enzyme isoforms, many others display mutations that involve catalytic residues. The latter ultimately code for catalytically inactive proteins with very high similarity to their active paralogs. These inactive members have been shown to be lectins, able to bind sialic acid and galactose in vitro, although their cellular functions are yet to be fully established. We now report structural and biochemical evidence extending the current molecular understanding of these lectins. We have solved the crystal structure of one such catalytically inactive trans-sialidase-like protein, after soaking with a specific carbohydrate ligand, sialyl-alpha2,3-lactose. Instead of the expected trisaccharide, the binding pocket was observed occupied by alpha-lactose, strongly suggesting that the protein retains residual hydrolytic activity. This hypothesis was validated by enzyme kinetics assays, in comparison to fully active wild-type trans-sialidase. Surface plasmon resonance also confirmed that these trans-sialidase-like lectins are not only able to bind small oligosaccharides, but also sialylated glycoproteins, which is relevant in the physiologic scenario of parasite infection. Inactive trans-sialidase proteins appear thus to be beta-methyl-galactosyl-specific lectins, evolved within an exo-sialidase scaffold, thus explaining why their lectin activity is triggered by the presence of terminal sialic acid.
Crystal structure of an enzymatically inactive trans-sialidase-like lectin from Trypanosoma cruzi: The carbohydrate binding mechanism involves residual sialidase activity.,Oppezzo P, Obal G, Baraibar MA, Pritsch O, Alzari PM, Buschiazzo A Biochim Biophys Acta. 2011 Apr 30. PMID:21570497[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Oppezzo P, Obal G, Baraibar MA, Pritsch O, Alzari PM, Buschiazzo A. Crystal structure of an enzymatically inactive trans-sialidase-like lectin from Trypanosoma cruzi: The carbohydrate binding mechanism involves residual sialidase activity. Biochim Biophys Acta. 2011 Apr 30. PMID:21570497 doi:10.1016/j.bbapap.2011.04.012
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