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| Title | CryoEM reveals the structure of an archaeal pilus involved in twitching motility. |
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| Journal, issue, pages | Nat Commun, Vol. 15, Issue 1, Page 5050, Year 2024 |
| Publish date | Jun 14, 2024 |
 Authors | Matthew C Gaines / Shamphavi Sivabalasarma / Michail N Isupov / Risat Ul Haque / Mathew McLaren / Cyril Hanus / Vicki A M Gold / Sonja-Verena Albers / Bertram Daum /    |
| PubMed Abstract | Amongst the major types of archaeal filaments, several have been shown to closely resemble bacterial homologues of the Type IV pili (T4P). Within Sulfolobales, member species encode for three types ...Amongst the major types of archaeal filaments, several have been shown to closely resemble bacterial homologues of the Type IV pili (T4P). Within Sulfolobales, member species encode for three types of T4P, namely the archaellum, the UV-inducible pilus system (Ups) and the archaeal adhesive pilus (Aap). Whereas the archaellum functions primarily in swimming motility, and the Ups in UV-induced cell aggregation and DNA-exchange, the Aap plays an important role in adhesion and twitching motility. Here, we present a cryoEM structure of the Aap of the archaeal model organism Sulfolobus acidocaldarius. We identify the component subunit as AapB and find that while its structure follows the canonical T4P blueprint, it adopts three distinct conformations within the pilus. The tri-conformer Aap structure that we describe challenges our current understanding of pilus structure and sheds new light on the principles of twitching motility. |
 External links | Nat Commun / PubMed:38877033 / PubMed Central |
| Methods | EM (helical sym.) |
| Resolution | 3.22 Å |
| Structure data | EMDB-18119, PDB-8q30: |
| Chemicals |  ChemComp-NAG: |
| Source |
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 Keywords | PROTEIN FIBRIL / cell surface appendage / N-glycosylation |
sulfolobus acidocaldarius (acidophilic)