8WX1
Cryo-EM structure of mouse SLC15A3 (outward-facing open)
Summary for 8WX1
| Entry DOI | 10.2210/pdb8wx1/pdb |
| EMDB information | 37897 |
| Descriptor | Solute carrier family 15 member 3 (1 entity in total) |
| Functional Keywords | transporter, membrane protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 64098.44 |
| Authors | Kasai, S.,Zhang, Z.,Ohto, U.,Shimizu, T. (deposition date: 2023-10-27, release date: 2024-10-30, Last modification date: 2025-07-02) |
| Primary citation | Zhang, Z.,Kasai, S.,Sakaniwa, K.,Fujimura, A.,Ohto, U.,Shimizu, T. The structures of the peptide transporters SLC15A3 and SLC15A4 reveal the recognition mechanisms for substrate and TASL. Structure, 33:330-, 2025 Cited by PubMed Abstract: The solute carrier family 15 members 3 and 4 (SLC15A3 and SLC15A4) are closely related endolysosomal peptide transporters that transport free histidine and certain dipeptides from the lumen to cytosol. Besides, SLC15A4 also functions as a scaffold protein for the recruitment of the adapter TASL for interferon regulatory factor 5 (IRF5) activation downstream of innate immune TLR7-9 signaling. However, the molecular basis for the substrate recognition and TASL recruitment by these membrane proteins is not well understood. Here, we report the cryoelectron microscopy (cryo-EM) structure of apo SLC15A3 and structures of SLC15A4 in the absence or presence of the substrate, revealing the specific dipeptide recognition mechanism. Each SLC15A3 and SLC15A4 protomer adopts an outward-facing conformation. Furthermore, we also present the cryo-EM structure of a SLC15A4-TASL complex. The N terminal region of TASL forms a helical structure that inserts deeply into the inward-facing cavity of SLC15A4. PubMed: 39719710DOI: 10.1016/j.str.2024.11.019 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.64 Å) |
Structure validation
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