{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gaines MC"],"funding":["EC | Horizon 2020 Framework Programme","Wellcome Trust","Biotechnology and Biological Sciences Research Council"],"pagination":["7411"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9715654"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["Pili are filamentous surface extensions that play roles in bacterial and archaeal cellular processes such as adhesion, biofilm formation, motility, cell-cell communication, DNA uptake and horizontal gene transfer. The model archaeaon Sulfolobus acidocaldarius assembles three filaments of the type-IV pilus superfamily (archaella, archaeal adhesion pili and UV-inducible pili), as well as a so-far uncharacterised fourth filament, named \"thread\". Here, we report on the cryo-EM structure of the archaeal thread. The filament is highly glycosylated and consists of subunits of the protein Saci_0406, arranged in a head-to-tail manner. Saci_0406 displays structural similarity, but low sequence homology, to bacterial type-I pilins. Thread subunits are interconnected via donor strand complementation, "],"journal":["Nature communications"],"pubmed_title":["Electron cryo-microscopy reveals the structure of the archaeal thread filament."],"pmcid":["PMC9715654"],"funding_grant_id":["803894","BB/R008639/1"],"pubmed_authors":["Isupov MN","Daum B","Gold VAM","McLaren M","Albers SV","Mollat CL","Haque RU","Neuhaus A","Sivabalasarma S","Tripp P","Gaines MC"],"additional_accession":[]},"is_claimable":false,"name":"Electron cryo-microscopy reveals the structure of the archaeal thread filament.","description":"Pili are filamentous surface extensions that play roles in bacterial and archaeal cellular processes such as adhesion, biofilm formation, motility, cell-cell communication, DNA uptake and horizontal gene transfer. The model archaeaon Sulfolobus acidocaldarius assembles three filaments of the type-IV pilus superfamily (archaella, archaeal adhesion pili and UV-inducible pili), as well as a so-far uncharacterised fourth filament, named \"thread\". Here, we report on the cryo-EM structure of the archaeal thread. The filament is highly glycosylated and consists of subunits of the protein Saci_0406, arranged in a head-to-tail manner. Saci_0406 displays structural similarity, but low sequence homology, to bacterial type-I pilins. Thread subunits are interconnected via donor strand complementation, ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-05-27T22:55:48.232Z","creation":"2025-04-06T12:12:14.371Z"},"accession":"S-EPMC9715654","cross_references":{"pubmed":["36456543"],"doi":["10.1038/s41467-022-34652-4"]}}