7ZW1
Human PRPH2-ROM1 hetero-dimer
Summary for 7ZW1
| Entry DOI | 10.2210/pdb7zw1/pdb |
| EMDB information | 14991 |
| Descriptor | Peripherin-2, Rod outer segment membrane protein 1, Nanobody (3 entities in total) |
| Functional Keywords | prph2, peripherin-2, rom1, hetero-complex, membrane protein, tetraspanin |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 91950.10 |
| Authors | |
| Primary citation | El Mazouni, D.,Gros, P. Cryo-EM structures of peripherin-2 and ROM1 suggest multiple roles in photoreceptor membrane morphogenesis. Sci Adv, 8:eadd3677-eadd3677, 2022 Cited by PubMed Abstract: Mammalian peripherin-2 (PRPH2) and rod outer segment membrane protein 1 (ROM1) are retina-specific tetraspanins that partake in the constant renewal of stacked membrane discs of photoreceptor cells that enable vision. Here, we present single-particle cryo-electron microscopy structures of solubilized PRPH2-ROM1 heterodimers and higher-order oligomers. High-risk PRPH2 and ROM1 mutations causing blindness map to the protein-dimer interface. Cysteine bridges connect dimers forming positive-curved oligomers, whereas negative-curved oligomers were observed occasionally. Hexamers and octamers exhibit a secondary micelle that envelopes four carboxyl-terminal helices, supporting a potential role in membrane remodeling. Together, the data indicate multiple structures for PRPH2-ROM1 in creating and maintaining compartmentalization of photoreceptor cells. PubMed: 36351012DOI: 10.1126/sciadv.add3677 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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