1ms3: Difference between revisions

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[[Image:1ms3.png|left|200px]]


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==Monoclinic form of Trypanosoma cruzi trans-sialidase==
The line below this paragraph, containing "STRUCTURE_1ms3", creates the "Structure Box" on the page.
<StructureSection load='1ms3' size='340' side='right'caption='[[1ms3]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
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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=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>
{{STRUCTURE_1ms3|  PDB=1ms3  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q26966_TRYCR Q26966_TRYCR]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ms/1ms3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1ms3 ConSurf].
<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.


===Monoclinic form of Trypanosoma cruzi trans-sialidase===
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>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12419220}}, adds the Publication Abstract to the page
*[[Neuraminidase 3D structures|Neuraminidase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12419220 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_12419220}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
[[1ms3]] is a 2 chain structure with sequence from [http://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].
 
==Reference==
<ref group="xtra">PMID:012419220</ref><ref group="xtra">PMID:019216574</ref><references group="xtra"/>
[[Category: Exo-alpha-sialidase]]
[[Category: Trypanosoma cruzi]]
[[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]]

Latest revision as of 10:02, 30 October 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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Buschiazzo A, Amaya MF, Cremona ML, Frasch AC, Alzari PM. The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis. Mol Cell. 2002 Oct;10(4):757-68. PMID:12419220

1ms3, resolution 1.65Å

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OCA