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{{STRUCTURE_4bkm|  PDB=4bkm  |  SCENE=  }}
==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]] 2.65&Aring;' scene=''>
{{ABSTRACT_PUBMED_24338473}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4bkm]] is a 4 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=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>
</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>
<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://www.rcsb.org/pdb/explore.do?structureId=4bkm RCSB], [http://www.ebi.ac.uk/pdbsum/4bkm PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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.


==Function==
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<ref>PMID:24338473</ref>
[[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).  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4bkm]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BKM OCA].
</div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:024338473</ref><references group="xtra"/><references/>
__TOC__
[[Category: Gohla, A.]]
</StructureSection>
[[Category: Knobloch, G.]]
[[Category: Lk3 transgenic mice]]
[[Category: Schindelin, H.]]
[[Category: Gohla, A]]
[[Category: Seifried, A.]]
[[Category: Knobloch, G]]
[[Category: Schindelin, H]]
[[Category: Seifried, A]]
[[Category: Had family]]
[[Category: Had family]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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