6y2v: Difference between revisions

New page: '''Unreleased structure''' The entry 6y2v is ON HOLD Authors: Levy, C. Description: Crystal structure of the double mutant L13R I16K of Low Molecular Weight Protein Tyrosine Phosphatas...
 
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'''Unreleased structure'''


The entry 6y2v is ON HOLD
==Crystal structure of the double mutant L13R I16K of Low Molecular Weight Protein Tyrosine Phosphatase (LMW-PTP)==
<StructureSection load='6y2v' size='340' side='right'caption='[[6y2v]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6y2v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y2V 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=PGE:TRIETHYLENE+GLYCOL'>PGE</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=6y2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y2v OCA], [https://pdbe.org/6y2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y2v RCSB], [https://www.ebi.ac.uk/pdbsum/6y2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y2v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PPAC_HUMAN PPAC_HUMAN] Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have used a combination of computational and structure-based redesign of the low molecular weight protein tyrosine phosphatase, LMW-PTP, to create new activity towards phosphoinositide substrates for which the wild-type enzyme had little or no activity. The redesigned enzymes retain catalytic activity despite residue alterations in the active site, and kinetic experiments confirmed specificity for up to four phosphoinositide substrates. Changes in the shape and overall volume of the active site where critical to facilitate access of the new substrates for catalysis. The kinetics data suggest that both the position and the combination of amino acid mutations are important for specificity towards the phosphoinositide substrates. The introduction of basic residues proved essential to establish new interactions with the multiple phosphate groups in the inositol head, thus promoting catalytically productive complexes. The crystallographic structures of the top-ranking designs confirmed the computational predictions and showed that residue substitutions do not alter the overall folding of the phosphatase or the conformation of the active site P-loop. The engineered LMW-PTP mutants with new activities can be useful reagents in investigating cell signalling pathways and offer the potential for therapeutic applications.


Authors: Levy, C.
Computational and structure-guided design of phosphoinositide substrate specificity into the tyrosine specific LMW-PTP enzyme.,Egbe E, Levy CW, Tabernero L PLoS One. 2020 Jun 25;15(6):e0235133. doi: 10.1371/journal.pone.0235133., eCollection 2020. PMID:32584877<ref>PMID:32584877</ref>


Description: Crystal structure of the double mutant L13R I16K of Low Molecular Weight Protein Tyrosine Phosphatase (LMW-PTP)
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Levy, C]]
<div class="pdbe-citations 6y2v" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Levy C]]

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