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-Structure paper
Title | Electron cryo-microscopy reveals the structure of the archaeal thread filament. |
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Journal, issue, pages | Nat Commun, Vol. 13, Issue 1, Page 7411, Year 2022 |
Publish date | Dec 1, 2022 |
Authors | Matthew C Gaines / Michail N Isupov / Shamphavi Sivabalasarma / Risat Ul Haque / Mathew McLaren / Clara L Mollat / Patrick Tripp / Alexander Neuhaus / Vicki A M Gold / Sonja-Verena Albers / Bertram Daum / |
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 ...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, a feature reminiscent of bacterial chaperone-usher pili. However, despite these similarities in overall architecture, archaeal threads appear to have evolved independently and are likely assembled by a distinct mechanism. |
External links | Nat Commun / PubMed:36456543 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 3.46 Å |
Structure data | EMDB-13546, PDB-7pnb: |
Source |
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Keywords | PROTEIN FIBRIL / cell surface appendage / beta-strand addition / isopeptide bond / N-glycosylation / beta-sandwich |