2i6p: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2i6p.jpg|left|200px]]<br /><applet load="2i6p" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2i6p, resolution 2.5&Aring;" />
-'''Crystal structure of the complex of the archaeal sulfolobus PTP-fold phosphatase with pNPP'''<br />
-==Overview==
+==Crystal structure of the complex of the archaeal sulfolobus PTP-fold phosphatase with pNPP==
-The P-loop-containing protein phos-phatases are important regulators in, signal transduction. These enzymes have structural and functional, similarity with a conserved sequence of Dx(25-41)HCxxGxxR(T/S) essential, for catalysis. The singular protein tyrosine phosphatase (PTP) from, archaeal Sulfolobus solfataricus is one of the smallest known PTPs with, extreme thermostability. Here, we report the crystal structure of this, phosphatase and its complexes with two tyrosyl phosphopeptides A-(p)Y-R, and N-K-(p)Y-G-N. The structure suggests the minimal structural motif of, the PTP family, having two variable sequences inserted between the, beta2-beta3 and beta3-beta4 strands, respectively. The phosphate of both, phosphopeptide substrates is bound to the P-loop through several hydrogen, bonds. Comparison of several phosphatase-substrate complexes revealed that, Gln135 on the Q-loop has different modes of recognition toward, phosphopeptides. The substrate specificity of SsoPTP is primarily, localized at the phosphotyrosine, suggesting that this phosphatase may be, a prototypical PTP. Proteins 2007. (c) 2006 Wiley-Liss, Inc.
+<StructureSection load='2i6p' size='340' side='right'caption='[[2i6p]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2i6p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I6P 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=4NP:4-NITROPHENYL+PHOSPHATE'>4NP</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=2i6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i6p OCA], [https://pdbe.org/2i6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i6p RCSB], [https://www.ebi.ac.uk/pdbsum/2i6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i6p ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q97VZ7_SACS2 Q97VZ7_SACS2]
+== 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/i6/2i6p_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=2i6p ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The P-loop-containing protein phos-phatases are important regulators in signal transduction. These enzymes have structural and functional similarity with a conserved sequence of Dx(25-41)HCxxGxxR(T/S) essential for catalysis. The singular protein tyrosine phosphatase (PTP) from archaeal Sulfolobus solfataricus is one of the smallest known PTPs with extreme thermostability. Here, we report the crystal structure of this phosphatase and its complexes with two tyrosyl phosphopeptides A-(p)Y-R and N-K-(p)Y-G-N. The structure suggests the minimal structural motif of the PTP family, having two variable sequences inserted between the beta2-beta3 and beta3-beta4 strands, respectively. The phosphate of both phosphopeptide substrates is bound to the P-loop through several hydrogen bonds. Comparison of several phosphatase-substrate complexes revealed that Gln135 on the Q-loop has different modes of recognition toward phosphopeptides. The substrate specificity of SsoPTP is primarily localized at the phosphotyrosine, suggesting that this phosphatase may be a prototypical PTP.
-==About this Structure==
+Enzyme-substrate interactions revealed by the crystal structures of the archaeal Sulfolobus PTP-fold phosphatase and its phosphopeptide complexes.,Chu HM, Wang AH Proteins. 2007 Mar 1;66(4):996-1003. PMID:17173287<ref>PMID:17173287</ref>
-I6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=4NP:'>4NP</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2I6P OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Enzyme-substrate interactions revealed by the crystal structures of the archaeal Sulfolobus PTP-fold phosphatase and its phosphopeptide complexes., Chu HM, Wang AH, Proteins. 2006 Dec 15;66(4):996-1003. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17173287 17173287]
+</div>
-[[Category: Protein-tyrosine-phosphatase]]
+<div class="pdbe-citations 2i6p" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
-[[Category: Sulfolobus solfataricus]]
-[[Category: Chu, H.M.]]
-[[Category: Wang, A.H.J.]]
-[[Category: 4NP]]
-[[Category: ptp domain]]
-[[Category: tyrosine phosphatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:35:59 2008''
+==See Also==
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saccharolobus solfataricus]]
+[[Category: Chu HM]]
+[[Category: Wang AHJ]]