3rl5

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Current revision (09:43, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3rl5' size='340' side='right'caption='[[3rl5]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
<StructureSection load='3rl5' size='340' side='right'caption='[[3rl5]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rl5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RL5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rl5]] 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=3RL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RL5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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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]] 1.26&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ib7|3ib7]], [[3ib8|3ib8]], [[2hy1|2hy1]], [[2hy0|2hy0]], [[2hyp|2hyp]], [[3rl4|3rl4]], [[3rl3|3rl3]]</div></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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mpped2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3rl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rl5 OCA], [https://pdbe.org/3rl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rl5 RCSB], [https://www.ebi.ac.uk/pdbsum/3rl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rl5 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=3rl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rl5 OCA], [https://pdbe.org/3rl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rl5 RCSB], [https://www.ebi.ac.uk/pdbsum/3rl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rl5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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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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[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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<div style="background-color:#fffaf0;">
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3rl5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dermol, U]]
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[[Category: Rattus norvegicus]]
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[[Category: Podobnik, M]]
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[[Category: Dermol U]]
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[[Category: Active site mutant]]
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[[Category: Podobnik M]]
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[[Category: Alpha-beta fold]]
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[[Category: Hydrolase]]
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[[Category: Metallophosphodiesterase]]
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[[Category: Single nucleotide polymorphism]]
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Current revision

Rat metallophosphodiesterase MPPED2 H67R Mutant

PDB ID 3rl5

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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