6CBC
Crystal structure of an N-terminal fragment of Vps13.
Summary for 6CBC
| Entry DOI | 10.2210/pdb6cbc/pdb |
| Descriptor | Vacuolar protein sorting-associated protein (1 entity in total) |
| Functional Keywords | lipid transfer protein, membrane trafficking, endoplasmic reticulum, mitochondria, endosomes, lipid binding protein |
| Biological source | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) |
| Total number of polymer chains | 2 |
| Total formula weight | 78468.95 |
| Authors | Kumar, N.,Horenkamp, F.A.,Reinisch, K.M. (deposition date: 2018-02-02, release date: 2018-08-08, Last modification date: 2024-10-09) |
| Primary citation | Kumar, N.,Leonzino, M.,Hancock-Cerutti, W.,Horenkamp, F.A.,Li, P.,Lees, J.A.,Wheeler, H.,Reinisch, K.M.,De Camilli, P. VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites. J. Cell Biol., 217:3625-3639, 2018 Cited by PubMed Abstract: 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. PubMed: 30093493DOI: 10.1083/jcb.201807019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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