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| | ==Crystal structure of the murine AUM (phosphoglycolate phosphatase) capping domain as a fusion protein with the catalytic core domain of murine chronophin (pyridoxal phosphate phosphatase)== | | ==Crystal structure of the murine AUM (phosphoglycolate phosphatase) capping domain as a fusion protein with the catalytic core domain of murine chronophin (pyridoxal phosphate phosphatase)== |
| - | <StructureSection load='4bkm' size='340' side='right' caption='[[4bkm]], [[Resolution|resolution]] 2.65Å' scene=''> | + | <StructureSection load='4bkm' size='340' side='right'caption='[[4bkm]], [[Resolution|resolution]] 2.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bkm]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BKM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BKM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bkm]] is a 4 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=4BKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BKM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 2.65Å</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=4bkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bkm OCA], [http://pdbe.org/4bkm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bkm RCSB], [http://www.ebi.ac.uk/pdbsum/4bkm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bkm ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=4bkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bkm OCA], [https://pdbe.org/4bkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bkm RCSB], [https://www.ebi.ac.uk/pdbsum/4bkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bkm 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).[https://www.uniprot.org/uniprot/PGP_MOUSE PGP_MOUSE] Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism (PubMed:26755581). Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear (PubMed:24338473, PubMed:26755581). In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (PubMed:24338473).<ref>PMID:24338473</ref> <ref>PMID:26755581</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Gohla, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Knobloch, G]] | + | [[Category: Mus musculus]] |
| - | [[Category: Schindelin, H]] | + | [[Category: Gohla A]] |
| - | [[Category: Seifried, A]] | + | [[Category: Knobloch G]] |
| - | [[Category: Had family]] | + | [[Category: Schindelin H]] |
| - | [[Category: Hydrolase]] | + | [[Category: Seifried A]] |
| Structural highlights
Function
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).PGP_MOUSE Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism (PubMed:26755581). Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear (PubMed:24338473, PubMed:26755581). In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (PubMed:24338473).[1] [2]
Publication Abstract from PubMed
Mammalian haloacid dehalogenase (HAD)-type phosphatases are an emerging family of phosphatases with important functions in physiology and disease, yet little is known about the basis of their substrate specificity. Here, we characterize a previously unexplored HAD family member (gene annotation: phosphoglycolate phosphatase) that we termed AUM, for aspartate-based, ubiquitous, Mg2+-dependent phosphatase. AUM is a tyrosine-specific paralog of the serine/threonine-specific protein and pyridoxal 5'-phosphate-directed HAD phosphatase chronophin. Comparative evolutionary and biochemical analyses reveal that a single, differently conserved residue in the cap domain of either AUM or chronophin is crucial for phosphatase specificity. We have solved the X-ray crystal structure of the AUM cap fused to the catalytic core of chronophin to 2.65 A resolution and present a detailed view of the catalytic clefts of AUM and chronophin that explains their substrate preferences. Our findings identify a small number of cap domain residues that encode the different substrate specificities of AUM and chronophin.
Evolutionary and Structural Analyses of the Mammalian Haloacid Dehalogenase-Type Phosphatases AUM and Chronophin Provide Insight into the Basis of their Different Substrate Specificities.,Seifried A, Knobloch G, Duraphe PS, Segerer G, Manhard J, Schindelin H, Schultz J, Gohla A J Biol Chem. 2013 Dec 13. PMID:24338473[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Seifried A, Knobloch G, Duraphe PS, Segerer G, Manhard J, Schindelin H, Schultz J, Gohla A. Evolutionary and Structural Analyses of the Mammalian Haloacid Dehalogenase-Type Phosphatases AUM and Chronophin Provide Insight into the Basis of their Different Substrate Specificities. J Biol Chem. 2013 Dec 13. PMID:24338473 doi:http://dx.doi.org/10.1074/jbc.M113.503359
- ↑ Mugabo Y, Zhao S, Seifried A, Gezzar S, Al-Mass A, Zhang D, Lamontagne J, Attane C, Poursharifi P, Iglesias J, Joly E, Peyot ML, Gohla A, Madiraju SR, Prentki M. Identification of a mammalian glycerol-3-phosphate phosphatase: Role in metabolism and signaling in pancreatic beta-cells and hepatocytes. Proc Natl Acad Sci U S A. 2016 Jan 26;113(4):E430-9. doi: , 10.1073/pnas.1514375113. Epub 2016 Jan 11. PMID:26755581 doi:http://dx.doi.org/10.1073/pnas.1514375113
- ↑ Seifried A, Knobloch G, Duraphe PS, Segerer G, Manhard J, Schindelin H, Schultz J, Gohla A. Evolutionary and Structural Analyses of the Mammalian Haloacid Dehalogenase-Type Phosphatases AUM and Chronophin Provide Insight into the Basis of their Different Substrate Specificities. J Biol Chem. 2013 Dec 13. PMID:24338473 doi:http://dx.doi.org/10.1074/jbc.M113.503359
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