5got: Difference between revisions

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-'''Unreleased structure'''
-The entry 5got is ON HOLD
+==Crystal structure of SP-PTP, low molecular weight protein tyrosine phosphatase from Streptococcus pyogenes==
+<StructureSection load='5got' size='340' side='right' caption='[[5got]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5got]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GOT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GOT FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5got FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5got OCA], [http://pdbe.org/5got PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5got RCSB], [http://www.ebi.ac.uk/pdbsum/5got PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5got ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Streptococcus pyogenes, or Group A Streptococcus (GAS), is a pathogenic bacterium that causes a variety of infectious diseases. The GAS genome encodes one protein tyrosine phosphatase, SP-PTP, which plays an essential role in the replication and virulence maintenance of GAS. Herein, we present the crystal structure of SP-PTP at 1.9 A resolution. Although SP-PTP has been reported to have dual phosphatase specificity for both phosphorylated tyrosine and serine/threonine, three-dimensional structural analysis showed that SP-PTP shares high similarity with typical low molecular weight protein tyrosine phosphatases (LMWPTPs), which are specific for phosphotyrosine, but not with dual-specificity phosphatases, in overall folding and active site composition. In the dephosphorylation activity test, SP-PTP consistently acted on phosphotyrosine substrates, but not or only minimally on phosphoserine/phosphothreonine substrates. Collectively, our structural and biochemical analyses verified SP-PTP as a canonical tyrosine-specific LMWPTP.
-Authors:
+Crystal structure of SP-PTP, a low molecular weight protein tyrosine phosphatase from Streptococcus pyogenes.,Ku B, Keum CW, Lee HS, Yun HY, Shin HC, Kim BY, Kim SJ Biochem Biophys Res Commun. 2016 Aug 19. pii: S0006-291X(16)31352-3. doi:, 10.1016/j.bbrc.2016.08.097. PMID:27545603<ref>PMID:27545603</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5got" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Protein-tyrosine-phosphatase]]
+[[Category: KIim, S J]]
+[[Category: Keum, C W]]
+[[Category: Ku, B]]
+[[Category: Hydrolase]]
+[[Category: Lmwptp]]
+[[Category: Sp-ptp]]
+[[Category: Streptococcus pyogene]]