8CTJ
Cryo-EM structure of TMEM87A
Summary for 8CTJ
| Entry DOI | 10.2210/pdb8ctj/pdb |
| EMDB information | 26992 |
| Descriptor | Transmembrane protein 87A, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (2 entities in total) |
| Functional Keywords | gold domain, transport, membrane protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 65256.92 |
| Authors | Hoel, C.M.,Zhang, L.,Brohawn, S.G. (deposition date: 2022-05-15, release date: 2022-07-20, Last modification date: 2022-11-30) |
| Primary citation | Hoel, C.M.,Zhang, L.,Brohawn, S.G. Structure of the GOLD-domain seven-transmembrane helix protein family member TMEM87A. Elife, 11:-, 2022 Cited by PubMed Abstract: TMEM87s are eukaryotic transmembrane proteins with two members (TMEM87A and TMEM87B) in humans. TMEM87s have proposed roles in protein transport to and from the Golgi, as mechanosensitive ion channels, and in developmental signaling. TMEM87 disruption has been implicated in cancers and developmental disorders. To better understand TMEM87 structure and function, we determined a cryo-EM structure of human TMEM87A in lipid nanodiscs. TMEM87A consists of a Golgi-dynamics (GOLD) domain atop a membrane-spanning seven-transmembrane helix domain with a large cavity open to solution and the membrane outer leaflet. Structural and functional analyses suggest TMEM87A may not function as an ion channel or G-protein coupled receptor. We find TMEM87A shares its characteristic domain arrangement with seven other proteins in humans; three that had been identified as evolutionary related (TMEM87B, GPR107, and GPR108) and four previously unrecognized homologs (GPR180, TMEM145, TMEM181, and WLS). Among these structurally related LD domain even-ransmembrane helix (GOST) proteins, WLS is best characterized as a membrane trafficking and secretion chaperone for lipidated Wnt signaling proteins. We find key structural determinants for WLS function are conserved in TMEM87A. We propose TMEM87A and structurally homologous GOST proteins could serve a common role in trafficking membrane-associated cargo. PubMed: 36373655DOI: 10.7554/eLife.81704 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.74 Å) |
Structure validation
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