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[[Image:2b4p.jpg|left|200px]]


{{Structure
==Structure of the D223N mutant of Selenomonas ruminantium PTP-like phytase==
|PDB= 2b4p |SIZE=350|CAPTION= <scene name='initialview01'>2b4p</scene>, resolution 1.81&Aring;
<StructureSection load='2b4p' size='340' side='right'caption='[[2b4p]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=MLI:MALONATE ION'>MLI</scene>
<table><tr><td colspan='2'>[[2b4p]] 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=2B4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B4P FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/5-phytase 5-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.72 3.1.3.72]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81&#8491;</td></tr>
|GENE= phyasr_R252K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=971 Selenomonas ruminantium])
<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></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=2b4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b4p OCA], [https://pdbe.org/2b4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b4p RCSB], [https://www.ebi.ac.uk/pdbsum/2b4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b4p 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/b4/2b4p_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=2b4p ConSurf].
<div style="clear:both"></div>


'''Structure of the D223N mutant of Selenomonas ruminantium PTP-like phytase'''
==See Also==
 
*[[Phytase 3D structures|Phytase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
2B4P is a [[Single protein]] structure of 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=2B4P OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17567745 17567745]
[[Category: 5-phytase]]
[[Category: Selenomonas ruminantium]]
[[Category: Selenomonas ruminantium]]
[[Category: Single protein]]
[[Category: Gruninger RJ]]
[[Category: Gruninger, R J.]]
[[Category: Mosimann SC]]
[[Category: Mosimann, S C.]]
[[Category: Selinger LB]]
[[Category: Selinger, L B.]]
[[Category: CL]]
[[Category: MLI]]
[[Category: ionic strength]]
[[Category: ptp-like]]
 
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Retrieved from "https://proteopedia.org/2b4p"