8OP4
Cryo-EM structure of P5A-ATPase CtSpf1 (E1-ATP state)
Summary for 8OP4
| Entry DOI | 10.2210/pdb8op4/pdb |
| Related | 8OP3 |
| EMDB information | 17039 17040 |
| Descriptor | Cation-transporting ATPase-like protein, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | translocase, membrane protein |
| Biological source | Thermochaetoides thermophila |
| Total number of polymer chains | 1 |
| Total formula weight | 149633.66 |
| Authors | Li, P.,Gourdon, P. (deposition date: 2023-04-06, release date: 2024-10-16, Last modification date: 2024-11-20) |
| Primary citation | Li, P.,Bagenholm, V.,Hagglund, P.,Lindkvist-Petersson, K.,Wang, K.,Gourdon, P. The structure and function of P5A-ATPases. Nat Commun, 15:9605-9605, 2024 Cited by PubMed Abstract: Endoplasmic reticulum (ER) membrane resident P5A-ATPases broadly affect protein biogenesis and quality control, and yet their molecular function remains debated. Here, we report cryo-EM structures of a P5A-ATPase, CtSpf1, covering multiple transport intermediates of the E1 → E1-ATP → E1P-ADP → E1P → E2P → E2.P → E2 → E1 cycle. In the E2P and E2.P states a cleft spans the entire membrane, holding a polypeptide cargo molecule. The cargo includes an ER luminal extension, pinpointed as the C-terminus in the E2.P state, which reenters the membrane in E2P. The E1 structure harbors a cytosol-facing cavity that is blocked by an insertion we refer to as the Plug-domain. The Plug-domain is nestled to key ATPase features and is displaced in the E1P-ADP and E1P states. Collectively, our findings are compatible with a broad range of proteins as cargo, with the P5A-ATPases serving a role in membrane removal of helices, although insertion/secretion cannot be excluded, as well as with a mechanistic role of the Plug-domain. PubMed: 39505844DOI: 10.1038/s41467-024-53757-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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