1ypt

<table><tr><td colspan='2'>[[1ypt]] is a 2 chain structure with sequence from [http://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=1YPT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YPT FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YOP51 ([http://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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ypt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ypt OCA], [http://pdbe.org/1ypt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ypt RCSB], [http://www.ebi.ac.uk/pdbsum/1ypt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ypt ProSAT]</span></td></tr>

[[http://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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== Publication Abstract from PubMed ==

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.

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:8052312<ref>PMID:8052312</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bacterium enterocoliticum schleifstein and coleman 1939]]

[[Category: Protein-tyrosine-phosphatase]]

[[Category: Dixon, J E]]

[[Category: Fauman, E B]]

[[Category: Saper, M A]]

[[Category: Schubert, H L]]

[[Category: Stuckey, J A]]

[[Category: Zhang, Z Y]]

[[Category: Protein tyrosine phosphatase]]