3u96: Difference between revisions

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<StructureSection load='3u96' size='340' side='right'caption='[[3u96]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3u96' size='340' side='right'caption='[[3u96]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3u96]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U96 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3u96]] is a 2 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=3U96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U96 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSN:N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM'>CSN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yop51, yopH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 "Bacterium enterocoliticum" Schleifstein and Coleman 1939])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSN:N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM'>CSN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=3u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u96 OCA], [https://pdbe.org/3u96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u96 RCSB], [https://www.ebi.ac.uk/pdbsum/3u96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u96 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=3u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u96 OCA], [https://pdbe.org/3u96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u96 RCSB], [https://www.ebi.ac.uk/pdbsum/3u96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u96 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.  
[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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Yersinia protein tyrosine phosphatase (YopH) is the most efficient enzyme among all PTPases. YopH is hyperactive compared to human PTPases, interfering with mammalian cellular pathways to achieve the pathogenicity of Yersinia. Two properties related to the catalytic loop structure differences have been proposed to affect its dynamics and enzyme efficiency. One is the ability of the loop to form stabilizing interactions to bound ligand after loop closure, which has long been recognized. In addition, the loop flexibility/mobility was suggested in a previous study to be a factor as well, based on the observation that incremental changes in PTPase loop structure by single point mutations to alanine often induce incremental changes in enzyme catalytic efficiency. In this study, the temperature jump relaxation spectroscopy (T-jump) has been used to discern the subtle changes of the loop dynamics due to point loop mutations. As expected, our results suggest a correlation between loop dynamics and the size of the residue on the catalytic loop. The stabilization of the enzyme-ligand complex is often enthalpy driven, achieved by formation of additional favorable hydrogen bonding/ionic interactions after loop closure. Interestingly, our T-jump and X-ray crystallography studies on YopH suggest that the elimination of some ligand-protein interactions by mutation does not necessarily destabilize the ligand-enzyme complex after loop closure, since the increased entropy in the forms of more mobile protein residues may be sufficient to compensate the free energy loss due to lost interactions and may even lead to enhanced efficiency of the enzyme catalysis. How these competing loop properties may affect loop dynamics and enzyme function are discussed.
 
Investigation of catalytic loop structure, dynamics, and function relationship of Yersinia protein tyrosine phosphatase by temperature-jump relaxation spectroscopy and X-ray structural determination.,Ke S, Ho MC, Zhadin N, Deng H, Callender R J Phys Chem B. 2012 May 31;116(21):6166-76. Epub 2012 May 22. PMID:22564106<ref>PMID:22564106</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3u96" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacterium enterocoliticum schleifstein and coleman 1939]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Yersinia enterocolitica]]
[[Category: Ho, M C]]
[[Category: Ho MC]]
[[Category: Ke, S]]
[[Category: Ke S]]
[[Category: Hydrolase]]
[[Category: Ptpase]]
[[Category: Yoph]]

Latest revision as of 11:38, 20 March 2024

Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCSCrystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS

Structural highlights

3u96 is a 2 chain structure with sequence from Yersinia enterocolitica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

See Also

3u96, resolution 1.80Å

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