6y2w - Revision history

OCA at 13:18, 24 January 2024

OCA — Wed, 24 Jan 2024 13:18:17 GMT

←Older revision		Revision as of 13:18, 24 January 2024
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	==Crystal structure of the single mutant I16K of Low Molecular Weight Protein Tyrosine Phosphatase (LMW-PTP)==		==Crystal structure of the single mutant I16K of Low Molecular Weight Protein Tyrosine Phosphatase (LMW-PTP)==
-	<StructureSection load='6y2w' size='340' side='right'caption='[[6y2w]]' scene=''>	+	<StructureSection load='6y2w' size='340' side='right'caption='[[6y2w]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y2W OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6Y2W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6y2w]] 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=6Y2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y2W FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6y2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y2w OCA], [~~http~~://pdbe.org/6y2w PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6y2w RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6y2w PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6y2w ProSAT]</span></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]] 1.77Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=6y2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y2w OCA], [https://pdbe.org/6y2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y2w RCSB], [https://www.ebi.ac.uk/pdbsum/6y2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y2w ProSAT]</span></td></tr>
	</table>		</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.
		+
		+	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>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6y2w" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Tyrosine phosphatase 3D structures\|Tyrosine phosphatase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Levy C]]		[[Category: Levy C]]

OCA at 10:56, 22 July 2020

OCA — Wed, 22 Jul 2020 10:56:05 GMT

←Older revision		Revision as of 10:56, 22 July 2020
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-	'''Unreleased structure'''

-	~~The entry 6y2w is ON HOLD until Paper Publication~~	+	==Crystal structure of the single mutant I16K of Low Molecular Weight Protein Tyrosine Phosphatase (LMW-PTP)==
-		+	<StructureSection load='6y2w' size='340' side='right'caption='[[6y2w]]' scene=''>
-	~~Authors: Levy, C.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y2W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Y2W FirstGlance]. <br>
-	~~Description:~~ Crystal structure of the single mutant I16K of Low Molecular Weight Protein Tyrosine Phosphatase (LMW-PTP)	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6y2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y2w OCA], [http://pdbe.org/6y2w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y2w RCSB], [http://www.ebi.ac.uk/pdbsum/6y2w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y2w ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: Levy, C]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Levy C]]

OCA at 05:42, 4 March 2020

OCA — Wed, 04 Mar 2020 05:42:50 GMT

←Older revision		Revision as of 05:42, 4 March 2020
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6y2w is ON HOLD	+	The entry 6y2w is ON HOLD until Paper Publication

	Authors: Levy, C.		Authors: Levy, C.

OCA: Protected "6y2w" [edit=sysop:move=sysop]

OCA — Wed, 26 Feb 2020 08:18:14 GMT

Protected "6y2w" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:18, 26 February 2020

OCA: New page: '''Unreleased structure''' The entry 6y2w is ON HOLD Authors: Levy, C. Description: Crystal structure of the single mutant I16K of Low Molecular Weight Protein Tyrosine Phosphatase (LM...

OCA — Wed, 26 Feb 2020 08:18:12 GMT

New page: '''Unreleased structure''' The entry 6y2w is ON HOLD Authors: Levy, C. Description: Crystal structure of the single mutant I16K of Low Molecular Weight Protein Tyrosine Phosphatase (LM...

New page

'''Unreleased structure'''

The entry 6y2w is ON HOLD

Authors: Levy, C.

Description: Crystal structure of the single mutant I16K of Low Molecular Weight Protein Tyrosine Phosphatase (LMW-PTP)
[[Category: Unreleased Structures]]
[[Category: Levy, C]]