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New page: left|200px<br /><applet load="1yts" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yts, resolution 2.5Å" /> '''A LIGAND-INDUCED CONF...
 
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[[Image:1yts.gif|left|200px]]<br /><applet load="1yts" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1yts, resolution 2.5&Aring;" />
'''A LIGAND-INDUCED CONFORMATIONAL CHANGE IN THE YERSINIA PROTEIN TYROSINE PHOSPHATASE'''<br />


==Overview==
==A LIGAND-INDUCED CONFORMATIONAL CHANGE IN THE YERSINIA PROTEIN TYROSINE PHOSPHATASE==
Protein tyrosine phosphatases (PTPases) play critical roles in the, intracellular signal transduction pathways that regulate cell, transformation, growth, and proliferation. The structures of several, different PTPases have revealed a conserved active site architecture in, which a phosphate-binding loop, together with an invariant arginine, cradle the phosphate of a phosphotyrosine substrate and poise it for, nucleophilic attack by an invariant cysteine nucleophile. We previously, reported that binding of tungstate to the Yop51 PTPase from Yersinia, induced a loop conformational change that moved aspartic acid 356 into the, active site, where it can function as a general acid. This is consistent, with the aspartic acid donating a proton to the tyrosyl leaving group, during the initial hydrolysis step. In this report, using a similar, structure of the inactive Cys 403--&gt;Ser mutant of the Yersinia PTPase, complexed with sulfate, we detail the structural and functional details of, this conformational change. In response to oxyanion binding, small, perturbations occur in active site residues, especially Arg 409, and, trigger the loop to close. Interestingly, the peptide bond following Asp, 356 has flipped to ligate a buried, active site water molecule that also, hydrogen bonds to the bound sulfate anion and two invariant glutamines., Loop closure also significantly decreases the solvent accessibility of the, bound oxyanion and could effectively shield catalytic intermediates from, phosphate acceptors other than water. We speculate that the intrinsic loop, flexibility of different PTPases may be related to their catalytic rate, and may play a role in the wide range of activities observed within this, enzyme family.
<StructureSection load='1yts' size='340' side='right'caption='[[1yts]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YTS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1yts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yts OCA], [https://pdbe.org/1yts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yts RCSB], [https://www.ebi.ac.uk/pdbsum/1yts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yts ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YOPH_YEREN YOPH_YEREN] Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages.
== 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/yt/1yts_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1yts ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1YTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YTS OCA].
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
A ligand-induced conformational change in the Yersinia protein tyrosine phosphatase., Schubert HL, Fauman EB, Stuckey JA, Dixon JE, Saper MA, Protein Sci. 1995 Sep;4(9):1904-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8528087 8528087]
[[Category: Large Structures]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Single protein]]
[[Category: Yersinia enterocolitica]]
[[Category: Yersinia enterocolitica]]
[[Category: Dixon, J.E.]]
[[Category: Dixon JE]]
[[Category: Fauman, E.B.]]
[[Category: Fauman EB]]
[[Category: Saper, M.A.]]
[[Category: Saper MA]]
[[Category: Schubert, H.L.]]
[[Category: Schubert HL]]
[[Category: Stuckey, J.A.]]
[[Category: Stuckey JA]]
[[Category: SO4]]
[[Category: protein tyrosine phosphatase]]
 
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Retrieved from "https://proteopedia.org/1yts"