1ypt

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(New page: 200px<br /><applet load="1ypt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ypt, resolution 2.5&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1ypt.gif|left|200px]]<br /><applet load="1ypt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ypt, resolution 2.5&Aring;" />
 
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'''CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE==
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Protein tyrosine phosphatases (PTPases) and kinases coregulate the, critical levels of phosphorylation necessary for intracellular signalling, cell growth and differentiation. Yersinia, the causative bacteria of the, bubonic plague and other enteric diseases, secrete an active PTPase, Yop51, that enters and suppresses host immune cells. Though the catalytic, domain is only approximately 20% identical to human PTP1B, the Yersinia, PTPase contains all of the invariant residues present in eukaryotic, PTPases, including the nucleophilic Cys 403 which forms a phosphocysteine, intermediate during catalysis. We present here structures of the, unliganded (2.5 A resolution) and tungstate-bound (2.6 A) crystal forms, which reveal that Cys 403 is positioned at the centre of a distinctive, phosphate-binding loop. This loop is at the hub of several hydrogen-bond, arrays that not only stabilize a bound oxyanion, but may activate Cys 403, as a reactive thiolate. Binding of tungstate triggers a conformational, change that traps the oxyanion and swings Asp 356, an important catalytic, residue, by approximately 6 A into the active site. The same anion-binding, loop in PTPases is also found in the enzyme rhodanese.
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<StructureSection load='1ypt' size='340' side='right'caption='[[1ypt]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ypt]] 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=1YPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YPT FirstGlance]. <br>
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</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>
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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=1ypt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ypt OCA], [https://pdbe.org/1ypt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ypt RCSB], [https://www.ebi.ac.uk/pdbsum/1ypt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ypt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yp/1ypt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1ypt ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1YPT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. 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=1YPT OCA].
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate., Stuckey JA, Schubert HL, Fauman EB, Zhang ZY, Dixon JE, Saper MA, Nature. 1994 Aug 18;370(6490):571-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8052312 8052312]
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[[Category: Large Structures]]
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Single protein]]
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[[Category: Yersinia enterocolitica]]
[[Category: Yersinia enterocolitica]]
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[[Category: Dixon, J.E.]]
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[[Category: Dixon JE]]
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[[Category: Fauman, E.B.]]
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[[Category: Fauman EB]]
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[[Category: Saper, M.A.]]
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[[Category: Saper MA]]
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[[Category: Schubert, H.L.]]
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[[Category: Schubert HL]]
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[[Category: Stuckey, J.A.]]
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[[Category: Stuckey JA]]
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[[Category: Zhang, Z.Y.]]
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[[Category: Zhang Z-Y]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:58:32 2007''
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Current revision

CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE

PDB ID 1ypt

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