ArticleProceedings of the National Academy of Sciences of the United States of America2026
Structural modeling reveals the mechanism of motor ATPase coordination during type IV pilus retraction.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Discovery of PilU as a second type IV pilus retraction motor inJournal of bacteriology · 2026Article
- Analysis of the heterogenous structural states of the hexameric ATPase PilU of the type IV pili from Vibrio cholerae.Protein science : a publication of the Protein Society · 2026Article
- Analysis of the heterogenous structural states of the hexameric ATPase PilU of the Type IV pili frombioRxiv : the preprint server for biology · 2026Article
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8 authors.
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Abstract
Diverse bacterial species utilize surface appendages called type IV pili (T4P) to interact with their environment. These structures are dynamically extended and retracted from the cell surface, which is critical for diverse functions. Some T4P systems rely on two distinct motor ATPases, PilT and PilU, whose combined activities are required to power forceful T4P retraction. However, the mechanism by which these motors coordinate to facilitate T4P retraction has remained unclear. Here, we utilize the competence T4P in
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