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==Structure of the PTP-like phytase from Selenomonas ruminantium in complex with myo-inositol (1,2,3,5,6)pentakisphosphate== | |||
<StructureSection load='3moz' size='340' side='right'caption='[[3moz]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3moz]] 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=3MOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MOZ 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]] 1.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5IP:(1R,2R,3R,4R,5S,6S)-6-HYDROXYCYCLOHEXANE-1,2,3,4,5-PENTAYL+PENTAKIS[DIHYDROGEN+(PHOSPHATE)]'>5IP</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3moz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3moz OCA], [https://pdbe.org/3moz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3moz RCSB], [https://www.ebi.ac.uk/pdbsum/3moz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3moz ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q7WUJ1_SELRU Q7WUJ1_SELRU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3moz" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phytase 3D structures|Phytase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Selenomonas ruminantium]] | |||
[[Category: Gruninger RJ]] | |||
[[Category: Mosimann SC]] | |||
[[Category: Selinger LB]] | |||
Latest revision as of 11:58, 6 September 2023
Structure of the PTP-like phytase from Selenomonas ruminantium in complex with myo-inositol (1,2,3,5,6)pentakisphosphateStructure of the PTP-like phytase from Selenomonas ruminantium in complex with myo-inositol (1,2,3,5,6)pentakisphosphate
Structural highlights
FunctionPublication Abstract from PubMedProtein-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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