4wty

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<StructureSection load='4wty' size='340' side='right'caption='[[4wty]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4wty' size='340' side='right'caption='[[4wty]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4wty]] is a 2 chain structure with sequence from [http://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=4WTY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WTY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4wty]] 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=4WTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WTY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mmj|3mmj]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phyA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=971 "Ancyromonas ruminantium" Certes 1889])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wty OCA], [https://pdbe.org/4wty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wty RCSB], [https://www.ebi.ac.uk/pdbsum/4wty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wty ProSAT]</span></td></tr>
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<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=4wty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wty OCA], [http://pdbe.org/4wty PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wty RCSB], [http://www.ebi.ac.uk/pdbsum/4wty PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wty ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q7WUJ1_SELRU Q7WUJ1_SELRU]
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Protein-tyrosine phosphatase-like inositol polyphosphatases are microbial enzymes that catalyze the stepwise removal of one or more phosphates from highly phosphorylated myo-inositols via a relatively ordered pathway. To understand the substrate specificity and kinetic mechanism of these enzymes we have determined high resolution, single crystal, x-ray crystallographic structures of inactive Selenomonas ruminantium PhyA in complex with myo-inositol hexa- and pentakisphosphate. These structures provide the first glimpse of a myo-inositol polyphosphatase-ligand complex consistent with its known specificity and reveal novel features of the kinetic mechanism. To complement the structural studies, fluorescent binding assays have been developed and demonstrate that the K(d) for this enzyme is several orders of magnitude lower than the K(m). Together with rapid kinetics data, these results suggest that the protein tyrosine phosphatase-like inositol polyphosphatases have a two-step, substrate-binding mechanism that facilitates catalysis.
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Substrate binding in protein-tyrosine phosphatase-like inositol polyphosphatases.,Gruninger RJ, Dobing S, Smith AD, Bruder LM, Selinger LB, Wieden HJ, Mosimann SC J Biol Chem. 2012 Mar 23;287(13):9722-30. doi: 10.1074/jbc.M111.309872. Epub 2011, Dec 2. PMID:22139834<ref>PMID:22139834</ref>
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==See Also==
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*[[Phytase 3D structures|Phytase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4wty" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ancyromonas ruminantium certes 1889]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bruder, L M]]
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[[Category: Selenomonas ruminantium]]
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[[Category: Mosimann, S C]]
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[[Category: Bruder LM]]
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[[Category: Hydrolase]]
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[[Category: Mosimann SC]]

Current revision

Structure of the PTP-like myo-inositol phosphatase from Selenomonas ruminantium in complex with myo-inositol-(1,3,4,5)-tetrakisphosphate

PDB ID 4wty

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