8XYJ
Structure of y+LAT1 bound with Lys
Summary for 8XYJ
| Entry DOI | 10.2210/pdb8xyj/pdb |
| EMDB information | 38775 |
| Descriptor | Y+L amino acid transporter 1, LYSINE (2 entities in total) |
| Functional Keywords | complex, membrane protein, amino acid |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 58110.33 |
| Authors | |
| Primary citation | Dai, L.,Zeng, Q.,Zhang, T.,Zhang, Y.,Shi, Y.,Li, Y.,Xu, K.,Huang, J.,Wang, Z.,Zhou, Q.,Yan, R. Structural basis for the substrate recognition and transport mechanism of the human y + LAT1-4F2hc transporter complex. Sci Adv, 11:eadq0558-eadq0558, 2025 Cited by PubMed Abstract: Heteromeric amino acid transporters (HATs), including yLAT1-4F2hc complex, are responsible for transporting amino acids across membranes, and mutations in yLAT1 cause lysinuric protein intolerance (LPI), a hereditary disorder characterized by defective cationic amino acid transport. The relationship between LPI and specific mutations in yLAT1 has yet to be fully understood. In this study, we characterized the function of yLAT1-4F2hc complex in mammalian cells and determined the cryo-EM structures of the human yLAT1-4F2hc complex in two distinct conformations: the apo state in an inward-open conformation and the native substrate-bound state in an outward-open conformation. Structural analysis suggests that Asp in yLAT1 plays a crucial role in coordination with sodium ion and substrate selectivity. Molecular dynamic (MD) simulations further revealed the different transport mechanism of cationic amino acids and neutral amino acids. These results provide important insights into the mechanisms of the substrate binding and working cycle of HATs. PubMed: 40106545DOI: 10.1126/sciadv.adq0558 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.33 Å) |
Structure validation
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