{"entity": "researcher", "timestamp": "2026-09-30T05:23:55.723Z", "family": "Matsuoka", "given": "Rei", "initials": "R", "orcid": "0000-0001-6718-2572", "affiliations": ["OMass Therapeutics Ltd, Building 4000, Chancellor Court, John Smith Drive, ARC Oxford, Oxford, UK."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/7f600c46b73f458ca4361ef58a78bb1c.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/7f600c46b73f458ca4361ef58a78bb1c"}}, "publications": [{"entity": "publication", "iuid": "d7a3c8344e5c41da9f113e5f966d348f", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/d7a3c8344e5c41da9f113e5f966d348f.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/d7a3c8344e5c41da9f113e5f966d348f"}}, "title": "Structural basis of specific lysine transport by Pseudomonas aeruginosa permease LysP.", "authors": [{"family": "Bicer", "given": "Deniz", "initials": "D"}, {"family": "Matsuoka", "given": "Rei", "initials": "R", "orcid": "0000-0001-6718-2572", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/7f600c46b73f458ca4361ef58a78bb1c.json"}}, {"family": "Moumbock", "given": "Aur\u00e9lien F A", "initials": "AFA", "orcid": "0000-0002-6034-2016", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/cdb85f0956bc46ccb33485a30d974635.json"}}, {"family": "Sukumar", "given": "Preethi", "initials": "P"}, {"family": "Suades", "given": "Albert", "initials": "A"}, {"family": "Cheruvara", "given": "Harish", "initials": "H"}, {"family": "Quigley", "given": "Andrew", "initials": "A", "orcid": "0000-0002-5022-9845", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/cbf31b2a111241debe003282b6188535.json"}}, {"family": "Drew", "given": "David", "initials": "D"}, {"family": "Pardon", "given": "Els", "initials": "E", "orcid": "0000-0002-2466-0172", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a7d3f1115bd141acbe7a45df09f97ecd.json"}}, {"family": "Steyaert", "given": "Jan", "initials": "J", "orcid": "0000-0002-3825-874X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b634e567865547b4abe67fa569f96a87.json"}}, {"family": "Henderson", "given": "Peter J F", "initials": "PJF", "orcid": "0000-0002-9187-0938", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ee0f4d3515f14b9dadfffa52aa0ad4e6.json"}}, {"family": "Caffrey", "given": "Martin", "initials": "M", "orcid": "0000-0002-2931-4551", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/44e3d483b2a644c2b2625640c7d6dc77.json"}}, {"family": "Griese", "given": "Julia J", "initials": "JJ", "orcid": "0000-0003-3686-3062", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/82045ff1a87e4f8997ef556daed43efa.json"}}, {"family": "Nji", "given": "Emmanuel", "initials": "E", "orcid": "0000-0001-6991-1046", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/daa539e0d91849c6801b6ad9c4c351c5.json"}}], "type": "journal article", "published": "2025-12-04", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "17", "issue": "1", "pages": "37", "issn-l": "2041-1723"}, "abstract": "Under conditions of extreme acidity, the lysine-specific permease, LysP, not only mediates the import of L-lysine it also interacts with the transcriptional regulator, CadC, to activate expression of the cadAB operon. This operon encodes the lysine decarboxylase, CadA, which converts lysine to cadaverine while consuming a cytoplasmic proton, and the antiporter, CadB, which exports protonated cadaverine in exchange for extracellular lysine. Together, these processes contribute to cytoplasmic pH homeostasis and support bacterial acid resistance - a mechanism essential for the survival of pathogenic bacteria in acidic host environments. Here, we present the cryo-EM structure of LysP from Pseudomonas aeruginosa in an inward-occluded conformation (3.2-5.3 \u00c5 resolution), bound to L-lysine and a nanobody. L-Lysine is coordinated by hydrophobic contacts, cation-\u03c0 interactions, and by hydrogen bonding mostly with polar uncharged residues. Reconstitution of LysP into proteoliposomes confirms specific L-lysine transport, which is competitively inhibited by L-4-thialysine. These findings provide a structural framework for understanding selective lysine recognition and inhibition, with implications for antibacterial drug design.", "doi": "10.1038/s41467-025-66618-7", "pmid": "41345107", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC12764776"}, {"db": "pii", "key": "10.1038/s41467-025-66618-7"}], "notes": [], "created": "2026-09-23T13:25:34.169Z", "modified": "2026-09-23T13:25:34.450Z"}]}