2b4u: Difference between revisions

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-[[Image:2b4u.png|left|200px]]
-{{STRUCTURE_2b4u|  PDB=2b4u  |  SCENE=  }}
+==Structure of the C252S mutant of Selenomonas ruminantium PTP-like phytase==
+<StructureSection load='2b4u' size='340' side='right'caption='[[2b4u]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2b4u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Selenomonas_ruminantium Selenomonas ruminantium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B4U 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&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2b4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b4u OCA], [https://pdbe.org/2b4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b4u RCSB], [https://www.ebi.ac.uk/pdbsum/2b4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b4u ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q7WUJ1_SELRU Q7WUJ1_SELRU]
+== 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/b4/2b4u_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2b4u ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+PhyA from Selenomonas ruminantium (PhyAsr), is a bacterial protein tyrosine phosphatase (PTP)-like inositol polyphosphate phosphatase (IPPase) that is distantly related to known PTPs. PhyAsr has a second substrate binding site referred to as a standby site and the P-loop (HCX5R) has been observed in both open (inactive) and closed (active) conformations. Site-directed mutagenesis and kinetic and structural studies indicate PhyAsr follows a classical PTP mechanism of hydrolysis and has a broad specificity toward polyphosphorylated myo-inositol substrates, including phosphoinositides. Kinetic and molecular docking experiments demonstrate PhyAsr preferentially cleaves the 3-phosphate position of Ins P6 and will produce Ins(2)P via a highly ordered series of sequential dephosphorylations: D-Ins(1,2,4,5,6)P5, Ins(2,4,5,6)P4, D-Ins(2,4,5)P3, and D-Ins(2,4)P2. The data support a distributive enzyme mechanism and suggest the PhyAsr standby site is involved in the recruitment of substrate. Structural studies at physiological pH and high salt concentrations demonstrate the "closed" or active P-loop conformation can be induced in the absence of substrate. These results suggest PhyAsr should be reclassified as a D-3 myo-inositol hexakisphosphate phosphohydrolase and suggest the PhyAsr reaction mechanism is more similar to that of PTPs than previously suspected.
-===Structure of the C252S mutant of Selenomonas ruminantium PTP-like phytase===
+Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase.,Puhl AA, Gruninger RJ, Greiner R, Janzen TW, Mosimann SC, Selinger LB Protein Sci. 2007 Jul;16(7):1368-78. Epub 2007 Jun 13. PMID:17567745<ref>PMID:17567745</ref>
-{{ABSTRACT_PUBMED_17567745}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2b4u" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[2b4u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Selenomonas_ruminantium Selenomonas ruminantium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B4U OCA].
+*[[Phytase 3D structures|Phytase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:017567745</ref><references group="xtra"/>
+__TOC__
-[[Category: 5-phytase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Selenomonas ruminantium]]
-[[Category: Gruninger, R J.]]
+[[Category: Gruninger RJ]]
-[[Category: Mosimann, S C.]]
+[[Category: Mosimann SC]]
-[[Category: Selinger, L B.]]
+[[Category: Selinger LB]]
-[[Category: Hydrolase]]
-[[Category: Ionic strength]]
-[[Category: Ptp-like]]