4bx3 - Revision history

OCA at 11:59, 20 December 2023

OCA — Wed, 20 Dec 2023 11:59:49 GMT

←Older revision		Revision as of 11:59, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bx3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BX3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bx3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BX3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.193Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4bx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bx3 OCA], [https://pdbe.org/4bx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bx3 RCSB], [https://www.ebi.ac.uk/pdbsum/4bx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bx3 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=4bx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bx3 OCA], [https://pdbe.org/4bx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bx3 RCSB], [https://www.ebi.ac.uk/pdbsum/4bx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bx3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PLPP_MOUSE PLPP_MOUSE]] Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP (By similarity).	+	[https://www.uniprot.org/uniprot/PLPP_MOUSE PLPP_MOUSE] Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Mammalian phosphatases of the haloacid dehalogenase (HAD) superfamily have emerged as important regulators of physiology and disease. Many of these enzymes are stable homodimers, yet the role of their dimerization is largely unknown. Here, we explore the function of the obligatory homodimerization of chronophin, a mammalian HAD phosphatase known to dephosphorylate pyridoxal 5'-phosphatase (PLP) and serine/threonine-phosphorylated proteins. The exchange of two residues in the murine chronophin homodimerization interface (chronophinAla194Lys, Ala195Lys; chronophinKK) yields a constitutive monomer, both in vitro and in cells. The catalytic activity of monomeric chronophin towards PLP is strongly impaired. X-ray crystallographic studies of chronophinKK reveal that dimer formation is essential for an intermolecular arginine-arginine-tryptophan stacking interaction that positions a critical histidine residue in the substrate specificity loop of chronophin for PLP coordination. Analysis of all available crystal structures of HAD hydrolases that are grouped together with chronophin in the C2a-type structural subfamily uncovers a highly conserved mode of dimerization that results in intermolecular contacts involving the substrate specificity loop. Our results explain how the dimerization of HAD hydrolases contributes to their catalytic efficiency and substrate specificity.
		+
		+	Chronophin dimerization is required for proper positioning of its substrate specificity loop.,Kestler C, Knobloch G, Tessmer I, Jeanclos E, Schindelin H, Gohla A J Biol Chem. 2013 Dec 14. PMID:24338687<ref>PMID:24338687</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4bx3" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:14, 7 September 2022

OCA — Wed, 07 Sep 2022 17:14:27 GMT

←Older revision		Revision as of 17:14, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4bx3' size='340' side='right'caption='[[4bx3]], [[Resolution\|resolution]] 2.19Å' scene=''>		<StructureSection load='4bx3' size='340' side='right'caption='[[4bx3]], [[Resolution\|resolution]] 2.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4bx3]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BX3 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4BX3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4bx3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BX3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bx0\|4bx0]], [[4bx2\|4bx2]]~~</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=4bx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bx3 OCA], [https://pdbe.org/4bx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bx3 RCSB], [https://www.ebi.ac.uk/pdbsum/4bx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bx3 ProSAT]</span></td></tr>
-	<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=4bx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bx3 OCA], [~~http~~://pdbe.org/4bx3 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4bx3 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4bx3 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4bx3 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PLPP_MOUSE PLPP_MOUSE]] Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP (By similarity).	+	[[https://www.uniprot.org/uniprot/PLPP_MOUSE PLPP_MOUSE]] Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP (By similarity).
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Mammalian phosphatases of the haloacid dehalogenase (HAD) superfamily have emerged as important regulators of physiology and disease. Many of these enzymes are stable homodimers, yet the role of their dimerization is largely unknown. Here, we explore the function of the obligatory homodimerization of chronophin, a mammalian HAD phosphatase known to dephosphorylate pyridoxal 5'-phosphatase (PLP) and serine/threonine-phosphorylated proteins. The exchange of two residues in the murine chronophin homodimerization interface (chronophinAla194Lys, Ala195Lys; chronophinKK) yields a constitutive monomer, both in vitro and in cells. The catalytic activity of monomeric chronophin towards PLP is strongly impaired. X-ray crystallographic studies of chronophinKK reveal that dimer formation is essential for an intermolecular arginine-arginine-tryptophan stacking interaction that positions a critical histidine residue in the substrate specificity loop of chronophin for PLP coordination. Analysis of all available crystal structures of HAD hydrolases that are grouped together with chronophin in the C2a-type structural subfamily uncovers a highly conserved mode of dimerization that results in intermolecular contacts involving the substrate specificity loop. Our results explain how the dimerization of HAD hydrolases contributes to their catalytic efficiency and substrate specificity.	+
-		+
-	Chronophin dimerization is required for proper positioning of its substrate specificity loop.,Kestler C, Knobloch G, Tessmer I, Jeanclos E, Schindelin H, Gohla A J Biol Chem. 2013 Dec 14. PMID:24338687<ref>PMID:24338687</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4bx3" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Gohla, A]]	+	[[Category: Gohla A]]
-	[[Category: Knobloch, G]]	+	[[Category: Knobloch G]]
-	[[Category: Schindelin, H]]	+	[[Category: Schindelin H]]
-	~~[[Category: Had phosphatase]]~~	+
-	~~[[Category: Had-like hydrolase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Pdxp~~]]	+

OCA at 13:19, 13 March 2019

OCA — Wed, 13 Mar 2019 13:19:02 GMT

←Older revision		Revision as of 13:19, 13 March 2019
Line 1:		Line 1:

	==Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)==		==Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)==
-	<StructureSection load='4bx3' size='340' side='right' caption='[[4bx3]], [[Resolution\|resolution]] 2.19Å' scene=''>	+	<StructureSection load='4bx3' size='340' side='right'caption='[[4bx3]], [[Resolution\|resolution]] 2.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bx3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BX3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bx3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BX3 FirstGlance]. <br>
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Gohla, A]]		[[Category: Gohla, A]]

OCA at 18:18, 4 August 2016

OCA — Thu, 04 Aug 2016 18:18:52 GMT

←Older revision		Revision as of 18:18, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)==		==Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)==
	<StructureSection load='4bx3' size='340' side='right' caption='[[4bx3]], [[Resolution\|resolution]] 2.19Å' scene=''>		<StructureSection load='4bx3' size='340' side='right' caption='[[4bx3]], [[Resolution\|resolution]] 2.19Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bx0\|4bx0]], [[4bx2\|4bx2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bx0\|4bx0]], [[4bx2\|4bx2]]</td></tr>
-	<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=4bx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bx3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bx3 RCSB], [http://www.ebi.ac.uk/pdbsum/4bx3 PDBsum]</span></td></tr>	+	<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=4bx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bx3 OCA], [http://pdbe.org/4bx3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bx3 RCSB], [http://www.ebi.ac.uk/pdbsum/4bx3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bx3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4bx3" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:07, 24 December 2014

OCA — Wed, 24 Dec 2014 18:07:40 GMT

←Older revision		Revision as of 18:07, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4bx3\| PDB=4bx3 \| SCENE= }}~~	+	==Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)==
-	===Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)===	+	<StructureSection load='4bx3' size='340' side='right' caption='[[4bx3]], [[Resolution\|resolution]] 2.19Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24338687}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4bx3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BX3 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bx0\|4bx0]], [[4bx2\|4bx2]]</td></tr>
		+	<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=4bx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bx3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bx3 RCSB], [http://www.ebi.ac.uk/pdbsum/4bx3 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/PLPP_MOUSE PLPP_MOUSE]] Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP (By similarity).		[[http://www.uniprot.org/uniprot/PLPP_MOUSE PLPP_MOUSE]] Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Mammalian phosphatases of the haloacid dehalogenase (HAD) superfamily have emerged as important regulators of physiology and disease. Many of these enzymes are stable homodimers, yet the role of their dimerization is largely unknown. Here, we explore the function of the obligatory homodimerization of chronophin, a mammalian HAD phosphatase known to dephosphorylate pyridoxal 5'-phosphatase (PLP) and serine/threonine-phosphorylated proteins. The exchange of two residues in the murine chronophin homodimerization interface (chronophinAla194Lys, Ala195Lys; chronophinKK) yields a constitutive monomer, both in vitro and in cells. The catalytic activity of monomeric chronophin towards PLP is strongly impaired. X-ray crystallographic studies of chronophinKK reveal that dimer formation is essential for an intermolecular arginine-arginine-tryptophan stacking interaction that positions a critical histidine residue in the substrate specificity loop of chronophin for PLP coordination. Analysis of all available crystal structures of HAD hydrolases that are grouped together with chronophin in the C2a-type structural subfamily uncovers a highly conserved mode of dimerization that results in intermolecular contacts involving the substrate specificity loop. Our results explain how the dimerization of HAD hydrolases contributes to their catalytic efficiency and substrate specificity.

-	~~==About this Structure==~~	+	Chronophin dimerization is required for proper positioning of its substrate specificity loop.,Kestler C, Knobloch G, Tessmer I, Jeanclos E, Schindelin H, Gohla A J Biol Chem. 2013 Dec 14. PMID:24338687<ref>PMID:24338687</ref>
-	~~[[4bx3]]~~ is ~~a 2 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4BX3 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024338687</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
-	[[Category: Gohla, A.]]	+	== References ==
-	[[Category: Knobloch, G.]]	+	<references/>
-	[[Category: Schindelin, H.]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Lk3 transgenic mice]]
		+	[[Category: Gohla, A]]
		+	[[Category: Knobloch, G]]
		+	[[Category: Schindelin, H]]
	[[Category: Had phosphatase]]		[[Category: Had phosphatase]]
	[[Category: Had-like hydrolase]]		[[Category: Had-like hydrolase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Pdxp]]		[[Category: Pdxp]]

OCA at 10:16, 25 December 2013

OCA — Wed, 25 Dec 2013 10:16:13 GMT

←Older revision		Revision as of 10:16, 25 December 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4bx3\| PDB=4bx3 \| SCENE= }}
		+	===Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)===
		+	{{ABSTRACT_PUBMED_24338687}}

-	~~The entry 4bx3 is ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/PLPP_MOUSE PLPP_MOUSE]] Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP (By similarity).

-	~~Authors~~: ~~Knobloch, G~~.~~, Gohla, A~~.~~, Schindelin, H~~.	+	==About this Structure==
		+	[[4bx3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BX3 OCA].

-	~~Description~~: ~~Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)~~	+	==Reference==
		+	<ref group="xtra">PMID:024338687</ref><references group="xtra"/><references/>
		+	[[Category: Gohla, A.]]
		+	[[Category: Knobloch, G.]]
		+	[[Category: Schindelin, H.]]
		+	[[Category: Had phosphatase]]
		+	[[Category: Had-like hydrolase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Pdxp]]

OCA at 07:10, 13 November 2013

OCA — Wed, 13 Nov 2013 07:10:26 GMT

←Older revision		Revision as of 07:10, 13 November 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4bx3 is ON HOLD	+	The entry 4bx3 is ON HOLD until Paper Publication

	Authors: Knobloch, G., Gohla, A., Schindelin, H.		Authors: Knobloch, G., Gohla, A., Schindelin, H.

	Description: Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)		Description: Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)

OCA: Protected "4bx3" [edit=sysop:move=sysop]

OCA — Thu, 18 Jul 2013 04:41:21 GMT

Protected "4bx3" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:41, 18 July 2013

OCA: New page: '''Unreleased structure''' The entry 4bx3 is ON HOLD Authors: Knobloch, G., Gohla, A., Schindelin, H. Description: Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphata...

OCA — Thu, 18 Jul 2013 04:41:20 GMT

New page: '''Unreleased structure''' The entry 4bx3 is ON HOLD Authors: Knobloch, G., Gohla, A., Schindelin, H. Description: Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphata...

New page

'''Unreleased structure'''

The entry 4bx3 is ON HOLD

Authors: Knobloch, G., Gohla, A., Schindelin, H.

Description: Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)