{"entity": "researcher", "timestamp": "2026-06-08T04:42:26.807Z", "family": "Meloni", "given": "Gabriele", "initials": "G", "orcid": "0000-0003-4976-1401", "affiliations": ["Department of Chemistry and Biochemistry, The University of Texas at Dallas, Richardson, United States."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/24f1558274e845e7a7351c62d8f627fe.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/24f1558274e845e7a7351c62d8f627fe"}}, "publications": [{"entity": "publication", "iuid": "35f8f501e005484788d085fd0b0a9d6f", "links": {"self": {"href": "https://publications.scilifelab.se/publication/35f8f501e005484788d085fd0b0a9d6f.json"}, "display": {"href": "https://publications.scilifelab.se/publication/35f8f501e005484788d085fd0b0a9d6f"}}, "title": "Closed and open structures of the eukaryotic magnesium channel Mrs2 reveal the auto-ligand-gating regulation mechanism.", "authors": [{"family": "Li", "given": "Ping", "initials": "P", "orcid": "0000-0002-7364-3301", "researcher": {"href": "https://publications.scilifelab.se/researcher/9cc17e1d61cb498b88038a9f5dfa6aff.json"}}, {"family": "Liu", "given": "Shiyan", "initials": "S"}, {"family": "Wallerstein", "given": "Johan", "initials": "J"}, {"family": "Villones", "given": "Rhiza Lyne E", "initials": "RLE"}, {"family": "Huang", "given": "Peng", "initials": "P"}, {"family": "Lindkvist-Petersson", "given": "Karin", "initials": "K", "orcid": "0000-0002-5209-3160", "researcher": {"href": "https://publications.scilifelab.se/researcher/efe1ac8c58f640ba98b97c6a5e52b9d5.json"}}, {"family": "Meloni", "given": "Gabriele", "initials": "G", "orcid": "0000-0003-4976-1401", "researcher": {"href": "https://publications.scilifelab.se/researcher/24f1558274e845e7a7351c62d8f627fe.json"}}, {"family": "Lu", "given": "Kefeng", "initials": "K", "orcid": "0000-0001-8200-9380", "researcher": {"href": "https://publications.scilifelab.se/researcher/d38d6efdc9744554b14b3370196467b8.json"}}, {"family": "Steen Jensen", "given": "Kristine", "initials": "K", "orcid": "0000-0001-9174-8361", "researcher": {"href": "https://publications.scilifelab.se/researcher/7b573ed9dbd440c6b4cda217120ff974.json"}}, {"family": "Liin", "given": "Sara I", "initials": "SI", "orcid": "0000-0001-8493-0114", "researcher": {"href": "https://publications.scilifelab.se/researcher/e82a591108f24dcabf50779d88fc8844.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": "2025-03-00", "journal": {"title": "Nat. Struct. Mol. Biol.", "issn": "1545-9985", "volume": "32", "issue": "3", "pages": "491-501", "issn-l": "1545-9985"}, "abstract": "The CorA/Mrs2 family of pentameric proteins are cardinal for the influx of Mg2+ across cellular membranes, importing the cation to mitochondria in eukaryotes. Yet, the conducting and regulation mechanisms of permeation remain elusive, particularly for the eukaryotic Mrs2 members. Here, we report closed and open Mrs2 cryo-electron microscopy structures, accompanied by functional characterization. Mg2+ flux is permitted by a narrow pore, gated by methionine and arginine residues in the closed state. Transition between the conformations is orchestrated by two pairs of conserved sensor-serving Mg2+-binding sites in the mitochondrial matrix lumen, located in between monomers. At lower levels of Mg2+, these ions are stripped, permitting an alternative, symmetrical shape, maintained by the RDLR motif that replaces one of the sensor site pairs in the open conformation. Thus, our findings collectively establish the molecular basis for selective Mg2+ influx of Mrs2 and an auto-ligand-gating regulation mechanism.", "doi": "10.1038/s41594-024-01432-1", "pmid": "39609652", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC11919701"}, {"db": "pii", "key": "10.1038/s41594-024-01432-1"}], "notes": [], "created": "2024-11-29T18:28:28.359Z", "modified": "2025-10-25T10:16:19.762Z"}, {"entity": "publication", "iuid": "59703b9ad74143418dad82d98296265a", "links": {"self": {"href": "https://publications.scilifelab.se/publication/59703b9ad74143418dad82d98296265a.json"}, "display": {"href": "https://publications.scilifelab.se/publication/59703b9ad74143418dad82d98296265a"}}, "title": "Structures of Atm1 provide insight into [2Fe-2S] cluster export from mitochondria.", "authors": [{"family": "Li", "given": "Ping", "initials": "P", "orcid": "0000-0002-7364-3301", "researcher": {"href": "https://publications.scilifelab.se/researcher/9cc17e1d61cb498b88038a9f5dfa6aff.json"}}, {"family": "Hendricks", "given": "Amber L", "initials": "AL"}, {"family": "Wang", "given": "Yong", "initials": "Y"}, {"family": "Villones", "given": "Rhiza Lyne E", "initials": "RLE"}, {"family": "Lindkvist-Petersson", "given": "Karin", "initials": "K", "orcid": "0000-0002-5209-3160", "researcher": {"href": "https://publications.scilifelab.se/researcher/efe1ac8c58f640ba98b97c6a5e52b9d5.json"}}, {"family": "Meloni", "given": "Gabriele", "initials": "G", "orcid": "0000-0003-4976-1401", "researcher": {"href": "https://publications.scilifelab.se/researcher/24f1558274e845e7a7351c62d8f627fe.json"}}, {"family": "Cowan", "given": "J A", "initials": "JA"}, {"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": "2022-07-27", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "13", "issue": "1", "pages": "4339", "issn-l": "2041-1723"}, "abstract": "In eukaryotes, iron-sulfur clusters are essential cofactors for numerous physiological processes, but these clusters are primarily biosynthesized in mitochondria. Previous studies suggest mitochondrial ABCB7-type exporters are involved in maturation of cytosolic iron-sulfur proteins. However, the molecular mechanism for how the ABCB7-type exporters participate in this process remains elusive. Here, we report a series of cryo-electron microscopy structures of a eukaryotic homolog of human ABCB7, CtAtm1, determined at average resolutions ranging from 2.8 to 3.2 \u00c5, complemented by functional characterization and molecular docking in silico. We propose that CtAtm1 accepts delivery from glutathione-complexed iron-sulfur clusters. A partially occluded state links cargo-binding to residues at the mitochondrial matrix interface that line a positively charged cavity, while the binding region becomes internalized and is partially divided in an early occluded state. Collectively, our findings substantially increase the understanding of the transport mechanism of eukaryotic ABCB7-type proteins.", "doi": "10.1038/s41467-022-32006-8", "pmid": "35896548", "labels": {"Cryo-EM": null}, "xrefs": [{"db": "pii", "key": "10.1038/s41467-022-32006-8"}, {"db": "pmc", "key": "PMC9329353"}], "notes": [], "created": "2022-08-01T10:18:17.525Z", "modified": "2024-11-07T08:45:00.230Z"}, {"entity": "publication", "iuid": "ce23ec6f017044b09f27dc1598fdefd5", "links": {"self": {"href": "https://publications.scilifelab.se/publication/ce23ec6f017044b09f27dc1598fdefd5.json"}, "display": {"href": "https://publications.scilifelab.se/publication/ce23ec6f017044b09f27dc1598fdefd5"}}, "title": "Structure and ion-release mechanism of PIB-4-type ATPases.", "authors": [{"family": "Gr\u00f8nberg", "given": "Christina", "initials": "C"}, {"family": "Hu", "given": "Qiaoxia", "initials": "Q"}, {"family": "Mahato", "given": "Dhani Ram", "initials": "DR", "orcid": "0000-0002-1121-7761", "researcher": {"href": "https://publications.scilifelab.se/researcher/a5b20e5b88984a1ebe80b1c49bbfc472.json"}}, {"family": "Longhin", "given": "Elena", "initials": "E"}, {"family": "Salustros", "given": "Nina", "initials": "N"}, {"family": "Duelli", "given": "Annette", "initials": "A"}, {"family": "Lyu", "given": "Pin", "initials": "P"}, {"family": "B\u00e5genholm", "given": "Viktoria", "initials": "V"}, {"family": "Eriksson", "given": "Jonas", "initials": "J"}, {"family": "Rao", "given": "Komal Umashankar", "initials": "KU"}, {"family": "Henderson", "given": "Domhnall Iain", "initials": "DI"}, {"family": "Meloni", "given": "Gabriele", "initials": "G", "orcid": "0000-0003-4976-1401", "researcher": {"href": "https://publications.scilifelab.se/researcher/24f1558274e845e7a7351c62d8f627fe.json"}}, {"family": "Andersson", "given": "Magnus", "initials": "M"}, {"family": "Croll", "given": "Tristan", "initials": "T"}, {"family": "Godaly", "given": "Gabriela", "initials": "G", "orcid": "0000-0002-3467-1350", "researcher": {"href": "https://publications.scilifelab.se/researcher/0caf97868fdc4a27a34006be81affb10.json"}}, {"family": "Wang", "given": "Kaituo", "initials": "K"}, {"family": "Gourdon", "given": "Pontus", "initials": "P", "orcid": "0000-0002-8631-3539", "researcher": {"href": "https://publications.scilifelab.se/researcher/3dc6cdbbcab048fab7a65df6cb796aab.json"}}], "type": "journal article", "published": "2021-12-24", "journal": {"title": "Elife", "issn": "2050-084X", "volume": "10", "issn-l": "2050-084X"}, "abstract": "Transition metals, such as zinc, are essential micronutrients in all organisms, but also highly toxic in excessive amounts. Heavy-metal transporting P-type (PIB) ATPases are crucial for homeostasis, conferring cellular detoxification and redistribution through transport of these ions across cellular membranes. No structural information is available for the PIB-4-ATPases, the subclass with the broadest cargo scope, and hence even their topology remains elusive. Here we present structures and complementary functional analyses of an archetypal PIB\u20114\u2011ATPase, sCoaT from Sulfitobacter sp. NAS14-1. The data disclose the architecture, devoid of classical so-called heavy metal binding domains, and provides fundamentally new insights into the mechanism and diversity of heavy-metal transporters. We reveal several novel P-type ATPase features, including a dual role in heavy-metal release and as an internal counter ion of an invariant histidine. We also establish that the turn-over of PIB\u2011ATPases is potassium independent, contrasting to many other P-type ATPases. Combined with new inhibitory compounds, our results open up for efforts in e.g. drug discovery, since PIB-4-ATPases function as virulence factors in many pathogens.", "doi": "10.7554/eLife.73124", "pmid": "34951590", "labels": {"Chemical Biology Consortium Sweden": "Collaborative"}, "xrefs": [{"db": "pii", "key": "73124"}], "notes": [], "created": "2022-01-20T10:44:18.963Z", "modified": "2025-10-17T13:04:27.980Z"}]}