8GMP
Cryo-EM structure of octameric human CALHM1 with a I109W point mutation
Summary for 8GMP
| Entry DOI | 10.2210/pdb8gmp/pdb |
| EMDB information | 40229 |
| Descriptor | Calcium homeostasis modulator protein 1, (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate (2 entities in total) |
| Functional Keywords | taste, assembly, calcium homeostasis modulator protein, membrane protein, channel, lipid binding, large-pore channel |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 8 |
| Total formula weight | 284820.92 |
| Authors | Syrjanen, J.L.,Furukawa, H. (deposition date: 2023-03-27, release date: 2023-07-26, Last modification date: 2024-10-30) |
| Primary citation | Syrjanen, J.L.,Epstein, M.,Gomez, R.,Furukawa, H. Structure of human CALHM1 reveals key locations for channel regulation and blockade by ruthenium red. Nat Commun, 14:3821-3821, 2023 Cited by PubMed Abstract: Calcium homeostasis modulator 1 (CALHM1) is a voltage-dependent channel involved in neuromodulation and gustatory signaling. Despite recent progress in the structural biology of CALHM1, insights into functional regulation, pore architecture, and channel blockade remain limited. Here we present the cryo-EM structure of human CALHM1, revealing an octameric assembly pattern similar to the non-mammalian CALHM1s and the lipid-binding pocket conserved across species. We demonstrate by MD simulations that this pocket preferentially binds a phospholipid over cholesterol to stabilize its structure and regulate the channel activities. Finally, we show that residues in the amino-terminal helix form the channel pore that ruthenium red binds and blocks. PubMed: 37380652DOI: 10.1038/s41467-023-39388-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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