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| | <StructureSection load='6cbc' size='340' side='right'caption='[[6cbc]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='6cbc' size='340' side='right'caption='[[6cbc]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6cbc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CBC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cbc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CBC FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0020450 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6cbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cbc OCA], [http://pdbe.org/6cbc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cbc RCSB], [http://www.ebi.ac.uk/pdbsum/6cbc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cbc 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=6cbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cbc OCA], [https://pdbe.org/6cbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cbc RCSB], [https://www.ebi.ac.uk/pdbsum/6cbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cbc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/VPS13_CHATD VPS13_CHATD] Mediates the transfer of lipids between membranes at organelle contact sites (By similarity). Binds phospholipids, including phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA), and phosphatidylserine (PS) (PubMed:30093493). May play a role in mitochondrial lipid homeostasis, Golgi vesicle transport, reticulophagy, actin cytoskeleton organization and formation of the prospore membrane (By similarity).[UniProtKB:Q07878]<ref>PMID:30093493</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Vacuolar protein sorting-associated protein|Vacuolar protein sorting-associated protein]] | + | *[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Horenkamp, F A]] | + | [[Category: Horenkamp FA]] |
| - | [[Category: Kumar, N]] | + | [[Category: Kumar N]] |
| - | [[Category: Reinisch, K M]] | + | [[Category: Reinisch KM]] |
| - | [[Category: Endoplasmic reticulum]]
| + | |
| - | [[Category: Endosome]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Lipid transfer protein]]
| + | |
| - | [[Category: Membrane trafficking]]
| + | |
| - | [[Category: Mitochondria]]
| + | |
| Structural highlights
Function
VPS13_CHATD Mediates the transfer of lipids between membranes at organelle contact sites (By similarity). Binds phospholipids, including phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA), and phosphatidylserine (PS) (PubMed:30093493). May play a role in mitochondrial lipid homeostasis, Golgi vesicle transport, reticulophagy, actin cytoskeleton organization and formation of the prospore membrane (By similarity).[UniProtKB:Q07878][1]
Publication Abstract from PubMed
Mutations in the human VPS13 genes are responsible for neurodevelopmental and neurodegenerative disorders including chorea acanthocytosis (VPS13A) and Parkinson's disease (VPS13C). The mechanisms of these diseases are unknown. Genetic studies in yeast hinted that Vps13 may have a role in lipid exchange between organelles. In this study, we show that the N-terminal portion of VPS13 is tubular, with a hydrophobic cavity that can solubilize and transport glycerolipids between membranes. We also show that human VPS13A and VPS13C bind to the ER, tethering it to mitochondria (VPS13A), to late endosome/lysosomes (VPS13C), and to lipid droplets (both VPS13A and VPS13C). These findings identify VPS13 as a lipid transporter between the ER and other organelles, implicating defects in membrane lipid homeostasis in neurological disorders resulting from their mutations. Sequence and secondary structure similarity between the N-terminal portions of Vps13 and other proteins such as the autophagy protein ATG2 suggest lipid transport roles for these proteins as well.
VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites.,Kumar N, Leonzino M, Hancock-Cerutti W, Horenkamp FA, Li P, Lees JA, Wheeler H, Reinisch KM, De Camilli P J Cell Biol. 2018 Oct 1;217(10):3625-3639. doi: 10.1083/jcb.201807019. Epub 2018 , Aug 9. PMID:30093493[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kumar N, Leonzino M, Hancock-Cerutti W, Horenkamp FA, Li P, Lees JA, Wheeler H, Reinisch KM, De Camilli P. VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites. J Cell Biol. 2018 Oct 1;217(10):3625-3639. doi: 10.1083/jcb.201807019. Epub 2018 , Aug 9. PMID:30093493 doi:http://dx.doi.org/10.1083/jcb.201807019
- ↑ Kumar N, Leonzino M, Hancock-Cerutti W, Horenkamp FA, Li P, Lees JA, Wheeler H, Reinisch KM, De Camilli P. VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites. J Cell Biol. 2018 Oct 1;217(10):3625-3639. doi: 10.1083/jcb.201807019. Epub 2018 , Aug 9. PMID:30093493 doi:http://dx.doi.org/10.1083/jcb.201807019
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