{"entity": "publication", "iuid": "484f789d5f624b5eb2c6700b353fef0a", "timestamp": "2026-07-22T14:26:50.595Z", "links": {"self": {"href": "https://publications.scilifelab.se/publication/484f789d5f624b5eb2c6700b353fef0a.json"}, "display": {"href": "https://publications.scilifelab.se/publication/484f789d5f624b5eb2c6700b353fef0a"}}, "title": "The structure and function of P5A-ATPases.", "authors": [{"family": "Li", "given": "Ping", "initials": "P", "orcid": "0000-0002-7364-3301", "researcher": {"href": "https://publications.scilifelab.se/researcher/9cc17e1d61cb498b88038a9f5dfa6aff.json"}}, {"family": "B\u00e5genholm", "given": "Viktoria", "initials": "V"}, {"family": "H\u00e4gglund", "given": "Per", "initials": "P", "orcid": "0000-0002-6627-7518", "researcher": {"href": "https://publications.scilifelab.se/researcher/e3f8312cdacb4d48b7c080e5fcc26959.json"}}, {"family": "Lindkvist-Petersson", "given": "Karin", "initials": "K", "orcid": "0000-0002-5209-3160", "researcher": {"href": "https://publications.scilifelab.se/researcher/efe1ac8c58f640ba98b97c6a5e52b9d5.json"}}, {"family": "Wang", "given": "Kaituo", "initials": "K", "orcid": "0000-0002-5922-7109", "researcher": {"href": "https://publications.scilifelab.se/researcher/0d8ad9a00c1c47fdbf1cadc149914823.json"}}, {"family": "Gourdon", "given": "Pontus", "initials": "P", "orcid": "0000-0002-8631-3539", "researcher": {"href": "https://publications.scilifelab.se/researcher/3dc6cdbbcab048fab7a65df6cb796aab.json"}}], "type": "journal article", "published": "2024-11-06", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "15", "issue": "1", "pages": "9605", "issn-l": "2041-1723"}, "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 \u2192 E1-ATP \u2192 E1P-ADP \u2192 E1P \u2192 E2P \u2192 E2.Pi \u2192 E2 \u2192 E1 cycle. In the E2P and E2.Pi 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.Pi 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.", "doi": "10.1038/s41467-024-53757-6", "pmid": "39505844", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41467-024-53757-6"}], "notes": [], "created": "2024-11-07T08:43:16.978Z", "modified": "2024-11-07T08:43:17.628Z"}