6cbc

Crystal structure of an N-terminal fragment of Vps13.

spinqualitylabelsall models 6cbc, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6cbc is a 2 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Vacuolar protein sorting-associated protein 3D structures

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