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| | <StructureSection load='2b4u' size='340' side='right'caption='[[2b4u]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2b4u' size='340' side='right'caption='[[2b4u]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2b4u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"ancyromonas_ruminantium"_certes_1889 "ancyromonas ruminantium" certes 1889]. 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> | + | <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='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=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2b4o|2b4o]], [[2b4p|2b4p]], [[1u24|1u24]], [[1u25|1u25]], [[1u26|1u26]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phyasr_C252S ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=971 "Ancyromonas ruminantium" Certes 1889])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/5-phytase 5-phytase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.72 3.1.3.72] </span></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> | | <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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7WUJ1_SELRU Q7WUJ1_SELRU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2b4u" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2b4u" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Phytase 3D structures|Phytase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ancyromonas ruminantium certes 1889]] | |
| - | [[Category: 5-phytase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gruninger, R J]] | + | [[Category: Selenomonas ruminantium]] |
| - | [[Category: Mosimann, S C]] | + | [[Category: Gruninger RJ]] |
| - | [[Category: Selinger, L B]] | + | [[Category: Mosimann SC]] |
| - | [[Category: Hydrolase]] | + | [[Category: Selinger LB]] |
| - | [[Category: Ionic strength]]
| + | |
| - | [[Category: Ptp-like]]
| + | |
| Structural highlights
Function
Q7WUJ1_SELRU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Puhl AA, Gruninger RJ, Greiner R, Janzen TW, Mosimann SC, Selinger LB. Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase. Protein Sci. 2007 Jul;16(7):1368-78. Epub 2007 Jun 13. PMID:17567745 doi:10.1110/ps.062738307
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