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5c16

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==Myotubularin-related proetin 1==
==Myotubularin-related proetin 1==
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<StructureSection load='5c16' size='340' side='right' caption='[[5c16]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
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<StructureSection load='5c16' size='340' side='right'caption='[[5c16]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5c16]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C16 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C16 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5c16]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C16 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.07&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol-3-phosphatase Phosphatidylinositol-3-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.64 3.1.3.64] </span></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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<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=5c16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c16 OCA], [http://pdbe.org/5c16 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c16 RCSB], [http://www.ebi.ac.uk/pdbsum/5c16 PDBsum]</span></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=5c16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c16 OCA], [https://pdbe.org/5c16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c16 RCSB], [https://www.ebi.ac.uk/pdbsum/5c16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c16 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MTMR1_HUMAN MTMR1_HUMAN]] Lipid phosphatase that has high specificity for phosphatidylinositol 3-phosphate and has no activity with phosphatidylinositol (3,5)-bisphosphate.<ref>PMID:11733541</ref>
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[https://www.uniprot.org/uniprot/MTMR1_HUMAN MTMR1_HUMAN] Lipid phosphatase that has high specificity for phosphatidylinositol 3-phosphate and has no activity with phosphatidylinositol (3,5)-bisphosphate.<ref>PMID:11733541</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Myotubularin-related protein 1 (MTMR1) is a phosphatase that belongs to the tyrosine/dual-specificity phosphatase superfamily. MTMR1 has been shown to use phosphatidylinositol 3-monophosphate (PI(3)P) and/or phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) as substrates. Here, we determined the crystal structure of human MTMR1. The refined model consists of the Pleckstrin homology (PH)-GRAM and phosphatase (PTP) domains. The overall structure was highly similar to the previously reported MTMR2 structure. Interestingly, two phosphate molecules were coordinated by strictly conserved residues located in the C(X)5R motif of the active site. Additionally, our biochemical studies confirmed the substrate specificity of MTMR1 for PI(3)P and PI(3,5)P2 over other phosphatidylinositol phosphates. Our structural and enzymatic analyses provide insight into the catalytic mechanism and biochemical properties of MTMR1.
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Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity.,Bong SM, Son KB, Yang SW, Park JW, Cho JW, Kim KT, Kim H, Kim SJ, Kim YJ, Lee BI PLoS One. 2016 Mar 28;11(3):e0152611. doi: 10.1371/journal.pone.0152611., eCollection 2016. PMID:27018598<ref>PMID:27018598</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 5c16" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Phosphatidylinositol-3-phosphatase]]
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[[Category: Homo sapiens]]
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[[Category: Bong, S M]]
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[[Category: Large Structures]]
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[[Category: Lee, B I]]
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[[Category: Bong SM]]
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[[Category: Hydrolase]]
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[[Category: Lee BI]]
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[[Category: Mtmr]]
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[[Category: Phosphatase]]
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Current revision

Myotubularin-related proetin 1

PDB ID 5c16

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