{"entity": "researcher", "timestamp": "2026-11-09T14:37:09.048Z", "family": "Kahle", "given": "Maximilian", "initials": "M", "orcid": "0000-0001-8942-8932", "affiliations": ["Institute of Biochemistry and Biology, Department of Biochemistry, University of Potsdam, Potsdam-Golm, Germany.", "Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/6a98b5bf1bcd4cd6b4b85546bc5044a3.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/6a98b5bf1bcd4cd6b4b85546bc5044a3"}}, "publications": [{"entity": "publication", "iuid": "4de9d9841cf74684a769e7ecbd2eded2", "links": {"self": {"href": "https://publications.scilifelab.se/publication/4de9d9841cf74684a769e7ecbd2eded2.json"}, "display": {"href": "https://publications.scilifelab.se/publication/4de9d9841cf74684a769e7ecbd2eded2"}}, "title": "NorQD AAA+ complex drives metal insertion by a twisting mechanism.", "authors": [{"family": "Kahle", "given": "Maximilian", "initials": "M", "orcid": "0000-0001-8942-8932", "researcher": {"href": "https://publications.scilifelab.se/researcher/6a98b5bf1bcd4cd6b4b85546bc5044a3.json"}}, {"family": "Appelgren", "given": "Sofia", "initials": "S", "orcid": "0000-0003-3175-6436", "researcher": {"href": "https://publications.scilifelab.se/researcher/231778f6f6b340d499d9db3d92f37d8b.json"}}, {"family": "K\u00f6nig", "given": "Finja", "initials": "F"}, {"family": "Carroni", "given": "Marta", "initials": "M", "orcid": "0000-0002-7697-6427", "researcher": {"href": "https://publications.scilifelab.se/researcher/e7f1bc1767024368abcb11a83184994a.json"}}, {"family": "\u00c4delroth", "given": "Pia", "initials": "P", "orcid": "0000-0003-0853-6785", "researcher": {"href": "https://publications.scilifelab.se/researcher/b798b3a524114a62b4132d17cb34f8ea.json"}}, {"family": "Wendler", "given": "Petra", "initials": "P", "orcid": "0000-0002-8285-2199", "researcher": {"href": "https://publications.scilifelab.se/researcher/c1d34f32d5e24165b51fcb399bc344e4.json"}}], "type": "journal article", "published": "2026-03-27", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "17", "issue": "1", "issn-l": "2041-1723"}, "abstract": "ATPases associated with diverse cellular activities (AAA+ -ATPases) catalyse a wide range of remodelling events in all phyla. AAA+ -ATPases of the MoxR-like family typically co-operate with von Willebrand factor type A (VWA) domain containing proteins to facilitate target remodelling and metal ion insertion, but their mechanism of action is poorly understood. We studied the bacterial AAA+ -ATPase NorQ in complex with its VWA domain partner protein NorD, which are essential for nitric oxide reductase (NOR) activity. Our cryo-EM structures and biochemical analyses show that NorQ and NorD engage through two key interfaces: (i) a finger-like extension protruding from the VWA domain that penetrates the central pore of the NorQ hexamer, and (ii) the NorD C- terminus, which contacts the post-sensor 1 loop of NorQ. Our data reveal that NorQ activity remodels a linker region in NorD essential for metal insertion. Together, these findings support a model in which the NorQ complex exerts a twisting and stretching force on the NorD linker, thereby enabling metal insertion into its target NOR.", "doi": "10.1038/s41467-026-71044-4", "pmid": "41896537", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC13036017"}, {"db": "pii", "key": "10.1038/s41467-026-71044-4"}], "notes": [], "created": "2026-11-05T14:00:03.673Z", "modified": "2026-11-05T14:00:03.803Z"}]}