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==Triclinic form of Trypanosoma cruzi trans-sialidase, in complex with lactose==
==Triclinic form of Trypanosoma cruzi trans-sialidase, in complex with lactose==
<StructureSection load='1ms9' size='340' side='right' caption='[[1ms9]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
<StructureSection load='1ms9' size='340' side='right'caption='[[1ms9]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ms9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Trycr Trycr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MS9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MS9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ms9]] 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=1MS9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MS9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</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]] 1.58&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mr5|1mr5]], [[1ms0|1ms0]], [[1ms1|1ms1]], [[1ms3|1ms3]], [[1ms4|1ms4]], [[1ms5|1ms5]], [[1ms8|1ms8]], [[1mz5|1mz5]], [[1mz6|1mz6]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</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=1ms9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ms9 OCA], [https://pdbe.org/1ms9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ms9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ms9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ms9 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=1ms9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ms9 OCA], [http://pdbe.org/1ms9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ms9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ms9 PDBsum]</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]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ms/1ms9_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ms/1ms9_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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=1ms9 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 1ms9" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Neuraminidase|Neuraminidase]]
*[[Neuraminidase 3D structures|Neuraminidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Exo-alpha-sialidase]]
[[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-acrbohydrate interaction]]
[[Category: Sialidase]]
[[Category: Trans-glycosylation]]

Latest revision as of 11:40, 10 April 2024

Triclinic form of Trypanosoma cruzi trans-sialidase, in complex with lactoseTriclinic form of Trypanosoma cruzi trans-sialidase, in complex with lactose

Structural highlights

1ms9 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 1.58Å
Ligands:, ,
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

1ms9, resolution 1.58Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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