1ms3: Difference between revisions

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<StructureSection load='1ms3' size='340' side='right'caption='[[1ms3]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='1ms3' size='340' side='right'caption='[[1ms3]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ms3]] is a 2 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=1MS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MS3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ms3]] is a 2 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=1MS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MS3 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mr5|1mr5]], [[1ms0|1ms0]], [[1ms1|1ms1]], [[1ms4|1ms4]], [[1ms5|1ms5]], [[1ms8|1ms8]], [[1ms9|1ms9]], [[1mz5|1mz5]], [[1mz6|1mz6]]</div></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]] 1.65&#8491;</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ms3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ms3 OCA], [https://pdbe.org/1ms3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ms3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ms3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ms3 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=1ms3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ms3 OCA], [https://pdbe.org/1ms3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ms3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ms3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ms3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q26966_TRYCR Q26966_TRYCR]
== 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=1ms3 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=1ms3 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Trans-sialidases (TS) are GPI-anchored surface enzymes expressed in specific developmental stages of trypanosome parasites like Trypanosoma cruzi, the etiologic agent of Chagas disease, and T. brucei, the causative agent of sleeping sickness. TS catalyzes the transfer of sialic acid residues from host to parasite glycoconjugates through a transglycosidase reaction that appears to be critical for T. cruzi survival and cell invasion capability. We report here the structure of the T. cruzi trans-sialidase, alone and in complex with sugar ligands. Sialic acid binding is shown to trigger a conformational switch that modulates the affinity for the acceptor substrate and concomitantly creates the conditions for efficient transglycosylation. The structure provides a framework for the structure-based design of novel inhibitors with potential therapeutic applications.
The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis.,Buschiazzo A, Amaya MF, Cremona ML, Frasch AC, Alzari PM Mol Cell. 2002 Oct;10(4):757-68. PMID:12419220<ref>PMID:12419220</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ms3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Neuraminidase 3D structures|Neuraminidase 3D structures]]
*[[Neuraminidase 3D structures|Neuraminidase 3D structures]]
== References ==
<references/>
__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: Amaya, M F]]
[[Category: Amaya MF]]
[[Category: Buschiazzo, A]]
[[Category: Buschiazzo A]]
[[Category: Cremona, M L]]
[[Category: Cremona ML]]
[[Category: Frasch, A C]]
[[Category: Frasch AC]]
[[Category: Beta-propeller]]
[[Category: Hydrolase]]
[[Category: Protein-carbohydrate interaction]]
[[Category: Sialidase]]
[[Category: Transglycosylation]]

Revision as of 11:40, 10 April 2024

Monoclinic form of Trypanosoma cruzi trans-sialidaseMonoclinic form of Trypanosoma cruzi trans-sialidase

Structural highlights

1ms3 is a 2 chain structure with sequence from Trypanosoma cruzi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q26966_TRYCR

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ms3, resolution 1.65Å

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OCA
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