6K9Y
Crystal structure of human VAT-1
Summary for 6K9Y
| Entry DOI | 10.2210/pdb6k9y/pdb |
| Descriptor | Synaptic vesicle membrane protein VAT-1 homolog, NITRATE ION (3 entities in total) |
| Functional Keywords | phospholipid transfer protein, oxidoreductase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 154358.34 |
| Authors | Watanabe, Y.,Endo, T. (deposition date: 2019-06-19, release date: 2020-02-12, Last modification date: 2023-11-22) |
| Primary citation | Watanabe, Y.,Tamura, Y.,Kakuta, C.,Watanabe, S.,Endo, T. Structural basis for interorganelle phospholipid transport mediated by VAT-1. J.Biol.Chem., 295:3257-3268, 2020 Cited by PubMed Abstract: Eukaryotic cells are compartmentalized to form organelles, whose functions rely on proper phospholipid and protein transport. Here we determined the crystal structure of human VAT-1, a cytosolic soluble protein that was suggested to transfer phosphatidylserine, at 2.2 Å resolution. We found that VAT-1 transferred not only phosphatidylserine but also other acidic phospholipids between membranes Structure-based mutational analyses showed the presence of a possible lipid-binding cavity at the interface between the two subdomains, and two tyrosine residues in the flexible loops facilitated phospholipid transfer, likely by functioning as a gate to this lipid-binding cavity. We also found that a basic and hydrophobic loop with two tryptophan residues protruded from the molecule and facilitated binding to the acidic-lipid membranes, thereby achieving efficient phospholipid transfer. PubMed: 32005660DOI: 10.1074/jbc.RA119.011019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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