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7cc7

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Tetratricopeptide repeat (TPR) domain of protein tyrosine phosphatase-interacting protein 51 (PTPIP51)

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Retrieved from "http://52.214.119.220/wiki/index.php/7cc7"

Categories: Homo sapiens | Large Structures | Lee BI | Park TH | Yeo HK

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 <StructureSection load='7cc7' size='340' side='right'caption='[[7cc7]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7cc7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CC7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7cc7]] is a 1 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=7CC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CC7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TSU:PARA-TOLUENE+SULFONATE'>TSU</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]] 1.45&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RMDN3, FAM82A2, FAM82C, PTPIP51, hucep-10, UNQ3122/PRO10274 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TSU:PARA-TOLUENE+SULFONATE'>TSU</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=7cc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cc7 OCA], [https://pdbe.org/7cc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cc7 RCSB], [https://www.ebi.ac.uk/pdbsum/7cc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cc7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/RMD3_HUMAN RMD3_HUMAN]] Involved in cellular calcium homeostasis regulation. May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis.<ref>PMID:16820967</ref> <ref>PMID:22131369</ref>
+[https://www.uniprot.org/uniprot/RMD3_HUMAN RMD3_HUMAN] Involved in cellular calcium homeostasis regulation. May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis.<ref>PMID:16820967</ref> <ref>PMID:22131369</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-In eukaryotic cells, mitochondria are closely tethered to the endoplasmic reticulum (ER) at sites called mitochondria-associated ER membranes (MAMs). Ca(2+) ion and phospholipid transfer occurs at MAMs to support diverse cellular functions. Unlike those in yeast, the protein complexes involved in phospholipid transfer at MAMs in humans have not been identified. Here, we determine the crystal structure of the tetratricopeptide repeat domain of PTPIP51 (PTPIP51_TPR), a mitochondrial protein that interacts with the ER-anchored VAPB protein at MAMs. The structure of PTPIP51_TPR shows an archetypal TPR fold, and an electron density map corresponding to an unidentified lipid-like molecule probably derived from the protein expression host is found in the structure. We reveal functions of PTPIP51 in phospholipid binding/transfer, particularly of phosphatidic acid, in vitro. Depletion of PTPIP51 in cells reduces the mitochondrial cardiolipin level. Additionally, we confirm that the PTPIP51-VAPB interaction is mediated by the FFAT-like motif of PTPIP51 and the MSP domain of VAPB. Our findings suggest that PTPIP51 is a phospholipid transfer protein with a MAM-tethering function.
-Phospholipid transfer function of PTPIP51 at mitochondria-associated ER membranes.,Yeo HK, Park TH, Kim HY, Jang H, Lee J, Hwang GS, Ryu SE, Park SH, Song HK, Ban HS, Yoon HJ, Lee BI EMBO Rep. 2021 May 2:e51323. doi: 10.15252/embr.202051323. PMID:33938112<ref>PMID:33938112</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7cc7" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Lee, B I]]
+[[Category: Lee BI]]
-[[Category: Park, T H]]
+[[Category: Park TH]]
-[[Category: Yeo, H K]]
+[[Category: Yeo HK]]
-[[Category: Endoplasmic reticulum]]
-[[Category: Lipid transport]]
-[[Category: Mam]]
-[[Category: Mitochondria]]
-[[Category: Phopsphplipid]]
-[[Category: Ptpip51]]
-[[Category: Tpr]]

7cc7

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Tetratricopeptide repeat (TPR) domain of protein tyrosine phosphatase-interacting protein 51 (PTPIP51)

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