{"entity": "researcher", "timestamp": "2026-08-07T18:26:14.347Z", "family": "Steyaert", "given": "Jan", "initials": "J", "orcid": "0000-0002-3825-874X", "affiliations": ["Structural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium.", "VIB-VUB Center for Structural Biology, VIB, Brussels, Belgium."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/2a13eb5511e1448fb982b5bd1bb1d6f1.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/2a13eb5511e1448fb982b5bd1bb1d6f1"}}, "publications": [{"entity": "publication", "iuid": "a37a5acc6c434e50afcfc8a6a13a8700", "links": {"self": {"href": "https://publications.scilifelab.se/publication/a37a5acc6c434e50afcfc8a6a13a8700.json"}, "display": {"href": "https://publications.scilifelab.se/publication/a37a5acc6c434e50afcfc8a6a13a8700"}}, "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.scilifelab.se/researcher/2ff469bc61824dfdbd2f1bd2d9eda8fb.json"}}, {"family": "Moumbock", "given": "Aur\u00e9lien F A", "initials": "AFA", "orcid": "0000-0002-6034-2016", "researcher": {"href": "https://publications.scilifelab.se/researcher/d82e18423c15489da2e66f44bc546208.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.scilifelab.se/researcher/3463df3e436f4accbef2c85d631d535b.json"}}, {"family": "Drew", "given": "David", "initials": "D"}, {"family": "Pardon", "given": "Els", "initials": "E", "orcid": "0000-0002-2466-0172", "researcher": {"href": "https://publications.scilifelab.se/researcher/375719a54c844150a4d5cb2b4f3ebb57.json"}}, {"family": "Steyaert", "given": "Jan", "initials": "J", "orcid": "0000-0002-3825-874X", "researcher": {"href": "https://publications.scilifelab.se/researcher/2a13eb5511e1448fb982b5bd1bb1d6f1.json"}}, {"family": "Henderson", "given": "Peter J F", "initials": "PJF", "orcid": "0000-0002-9187-0938", "researcher": {"href": "https://publications.scilifelab.se/researcher/9a039ab6f9b946079084fa5c5a1d73cb.json"}}, {"family": "Caffrey", "given": "Martin", "initials": "M", "orcid": "0000-0002-2931-4551", "researcher": {"href": "https://publications.scilifelab.se/researcher/4860054d06e24ccfb39fe781305f73d8.json"}}, {"family": "Griese", "given": "Julia J", "initials": "JJ", "orcid": "0000-0003-3686-3062", "researcher": {"href": "https://publications.scilifelab.se/researcher/308d2df438d8443ca932fb5111e4590e.json"}}, {"family": "Nji", "given": "Emmanuel", "initials": "E", "orcid": "0000-0001-6991-1046", "researcher": {"href": "https://publications.scilifelab.se/researcher/88dfdecdfcb44a97b8513508e294aebd.json"}}], "type": "journal article", "published": "2025-12-04", "journal": {"title": "Nat Commun", "issn": "2041-1723", "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": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41467-025-66618-7"}], "notes": [], "created": "2025-12-09T13:04:51.180Z", "modified": "2025-12-09T13:04:57.345Z"}, {"entity": "publication", "iuid": "32532dfcd911424f93ddea636563394f", "links": {"self": {"href": "https://publications.scilifelab.se/publication/32532dfcd911424f93ddea636563394f.json"}, "display": {"href": "https://publications.scilifelab.se/publication/32532dfcd911424f93ddea636563394f"}}, "title": "Snapshots of actin and tubulin folding inside the TRiC chaperonin.", "authors": [{"family": "Kelly", "given": "John J", "initials": "JJ"}, {"family": "Tranter", "given": "Dale", "initials": "D"}, {"family": "Pardon", "given": "Els", "initials": "E", "orcid": "0000-0002-2466-0172", "researcher": {"href": "https://publications.scilifelab.se/researcher/375719a54c844150a4d5cb2b4f3ebb57.json"}}, {"family": "Chi", "given": "Gamma", "initials": "G"}, {"family": "Kramer", "given": "Holger", "initials": "H", "orcid": "0000-0002-6400-0945", "researcher": {"href": "https://publications.scilifelab.se/researcher/cf9fb27444604e999fe8815be9eb336a.json"}}, {"family": "Happonen", "given": "Lotta", "initials": "L", "orcid": "0000-0002-5922-4549", "researcher": {"href": "https://publications.scilifelab.se/researcher/a7af0a6faf6a48e7937a644be472edbe.json"}}, {"family": "Knee", "given": "Kelly M", "initials": "KM"}, {"family": "Janz", "given": "Jay M", "initials": "JM"}, {"family": "Steyaert", "given": "Jan", "initials": "J", "orcid": "0000-0002-3825-874X", "researcher": {"href": "https://publications.scilifelab.se/researcher/2a13eb5511e1448fb982b5bd1bb1d6f1.json"}}, {"family": "Bulawa", "given": "Christine", "initials": "C"}, {"family": "Paavilainen", "given": "Ville O", "initials": "VO", "orcid": "0000-0002-3160-7767", "researcher": {"href": "https://publications.scilifelab.se/researcher/f76359e8b92b4b53af80c36d064a1a42.json"}}, {"family": "Huiskonen", "given": "Juha T", "initials": "JT", "orcid": "0000-0002-0348-7323", "researcher": {"href": "https://publications.scilifelab.se/researcher/c858a2e60971462f9e53653320c9eb0f.json"}}, {"family": "Yue", "given": "Wyatt W", "initials": "WW", "orcid": "0000-0001-6959-6007", "researcher": {"href": "https://publications.scilifelab.se/researcher/5be92e7076054a009efe9d23f78b5a48.json"}}], "type": "journal article", "published": "2022-04-21", "journal": {"title": "Nat. Struct. Mol. Biol.", "issn": "1545-9985", "issn-l": "1545-9985"}, "abstract": "The integrity of a cell's proteome depends on correct folding of polypeptides by chaperonins. The chaperonin TCP-1 ring complex (TRiC) acts as obligate folder for >10% of cytosolic proteins, including he cytoskeletal proteins actin and tubulin. Although its architecture and how it recognizes folding substrates are emerging from structural studies, the subsequent fate of substrates inside the TRiC chamber is not defined. We trapped endogenous human TRiC with substrates (actin, tubulin) and cochaperone (PhLP2A) at different folding stages, for structure determination by cryo-EM. The already-folded regions of client proteins are anchored at the chamber wall, positioning unstructured regions toward the central space to achieve their native fold. Substrates engage with different sections of the chamber during the folding cycle, coupled to TRiC open-and-close transitions. Further, the cochaperone PhLP2A modulates folding, acting as a molecular strut between substrate and TRiC chamber. Our structural snapshots piece together an emerging model of client protein folding within TRiC.", "doi": "10.1038/s41594-022-00755-1", "pmid": "35449234", "labels": {"Structural Proteomics": "Collaborative"}, "xrefs": [{"db": "pii", "key": "10.1038/s41594-022-00755-1"}], "notes": [], "created": "2022-04-27T14:22:02.454Z", "modified": "2022-04-27T14:22:02.677Z"}]}