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3rl4

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==Rat metallophosphodiesterase MPPED2 G252H Mutant==
==Rat metallophosphodiesterase MPPED2 G252H Mutant==
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<StructureSection load='3rl4' size='340' side='right' caption='[[3rl4]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
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<StructureSection load='3rl4' size='340' side='right'caption='[[3rl4]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rl4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RL4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RL4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rl4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RL4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RL4 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.29&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ib7|3ib7]], [[3ib8|3ib8]], [[2hy1|2hy1]], [[2hy0|2hy0]], [[2hyp|2hyp]], [[3rl3|3rl3]], [[3rl5|3rl5]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mpped2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rl4 OCA], [https://pdbe.org/3rl4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rl4 RCSB], [https://www.ebi.ac.uk/pdbsum/3rl4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rl4 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rl4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rl4 RCSB], [http://www.ebi.ac.uk/pdbsum/3rl4 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/MPPD2_RAT MPPD2_RAT] Displays low metallophosphoesterase activity (in vitro). May play a role in the development of the nervous system.
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== Publication Abstract from PubMed ==
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Metallophosphoesterase-domain-containing protein 2 (MPPED2) is a highly evolutionarily conserved protein with orthologs found from worms to humans. The human MPPED2 gene is found in a region of chromosome 11 that is deleted in patients with WAGR (Wilms tumor, aniridia, genitourinary anomalies, and mental retardation) syndrome, and MPPED2 may function as a tumor suppressor. However, the precise cellular roles of MPPED2 are unknown, and its low phosphodiesterase activity suggests that substrate hydrolysis may not be its prime function. We present here the structures of MPPED2 and two mutants, which show that the poor activity of MPPED2 is not only a consequence of the substitution of an active-site histidine residue by glycine but also due to binding of AMP or GMP to the active site. This feature, enhanced by structural elements of the protein, allows MPPED2 to utilize the conserved phosphoprotein-phosphatase-like fold in a unique manner, ensuring that its enzymatic activity can be combined with a possible role as a scaffolding or adaptor protein.
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Unique utilization of a phosphoprotein phosphatase fold by a mammalian phosphodiesterase associated with WAGR syndrome.,Dermol U, Janardan V, Tyagi R, Visweswariah SS, Podobnik M J Mol Biol. 2011 Sep 23;412(3):481-94. Epub 2011 Jul 30. PMID:21824479<ref>PMID:21824479</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Dermol, U.]]
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[[Category: Dermol U]]
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[[Category: Podobnik, M.]]
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[[Category: Podobnik M]]
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[[Category: Active site mutant]]
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[[Category: Alpha-beta fold]]
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[[Category: Gmp]]
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[[Category: Hydrolase]]
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[[Category: Metallophosphodiesterase]]
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Current revision

Rat metallophosphodiesterase MPPED2 G252H Mutant

PDB ID 3rl4

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