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TitleStructural basis for the substrate recognition and transport mechanism of the human yLAT1-4F2hc transporter complex.
Journal, issue, pagesSci Adv, Vol. 11, Issue 12, Page eadq0558, Year 2025
Publish dateMar 21, 2025
AuthorsLu Dai / Qian Zeng / Ting Zhang / Yuanyuan Zhang / Yi Shi / Yaning Li / Kangtai Xu / Jing Huang / Zilong Wang / Qiang Zhou / Renhong Yan /
PubMed AbstractHeteromeric amino acid transporters (HATs), including yLAT1-4F2hc complex, are responsible for transporting amino acids across membranes, and mutations in yLAT1 cause lysinuric protein intolerance ...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.
External linksSci Adv / PubMed:40106545 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.74 Å
Structure data

38750

8xxi

EMDB-38750, PDB-8xxi:
Structure of y+LAT1 bound with Leu
Method: EM (single particle) / Resolution: 3.04 Å

38775

8xyj

EMDB-38775, PDB-8xyj:
Structure of y+LAT1 bound with Lys
Method: EM (single particle) / Resolution: 3.33 Å

39388

8ylp

EMDB-39388, PDB-8ylp:
Overall structure of the y+LAT1-4F2hc bound with Arg
Method: EM (single particle) / Resolution: 2.9 Å

62332

9kh5

EMDB-62332, PDB-9kh5:
Structure of y+LAT1
Method: EM (single particle) / Resolution: 3.74 Å

62377

9kju

EMDB-62377, PDB-9kju:
Local refinement of the y+LAT1-4F2hc bound with Arg
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-LEU:
LEUCINE

ChemComp-LYS:
LYSINE

ChemComp-ARG:
ARGININE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / complex / amino acid

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