Unknown

Dataset Information

0

Structural basis for interorganelle phospholipid transport mediated by VAT-1.


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 in vitro 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.

SUBMITTER: Watanabe Y 

PROVIDER: S-EPMC7062155 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC5759761 | biostudies-literature
| S-EPMC7797000 | biostudies-literature
| S-EPMC4515121 | biostudies-literature
| S-EPMC9239997 | biostudies-literature
| S-EPMC6508934 | biostudies-literature
| S-EPMC11289387 | biostudies-literature
| S-EPMC8617236 | biostudies-literature
| S-EPMC7822847 | biostudies-literature
| S-EPMC6114099 | biostudies-literature
2018-01-01 | GSE99391 | GEO