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-Structure paper
Title | Structural mechanisms of Tad pilus assembly and its interaction with an RNA virus. |
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Journal, issue, pages | Sci Adv, Vol. 10, Issue 18, Page eadl4450, Year 2024 |
Publish date | May 3, 2024 |
Authors | Yuhang Wang / Matthew Theodore / Zhongliang Xing / Utkarsh Narsaria / Zihao Yu / Lanying Zeng / Junjie Zhang / |
PubMed Abstract | Tad (tight adherence) pili, part of the type IV pili family, are crucial for mechanosensing, surface adherence, bacteriophage (phage) adsorption, and cell-cycle regulation. Unlike other type IV ... Tad (tight adherence) pili, part of the type IV pili family, are crucial for mechanosensing, surface adherence, bacteriophage (phage) adsorption, and cell-cycle regulation. Unlike other type IV pilins, Tad pilins lack the typical globular β sheet domain responsible for pilus assembly and phage binding. The mechanisms of Tad pilus assembly and its interaction with phage ΦCb5 have been elusive. Using cryo-electron microscopy, we unveiled the Tad pilus assembly mechanism, featuring a unique network of hydrogen bonds at its core. We then identified the Tad pilus binding to the ΦCb5 maturation protein (Mat) through its β region. Notably, the amino terminus of ΦCb5 Mat is exposed outside the capsid and phage/pilus interface, enabling the attachment of fluorescent and affinity tags. These engineered ΦCb5 virions can be efficiently assembled and purified in , maintaining infectivity against , which presents promising applications, including RNA delivery and phage display. |
External links | Sci Adv / PubMed:38701202 / PubMed Central |
Methods | EM (helical sym.) / EM (single particle) |
Resolution | 2.7 - 6.45 Å |
Structure data | EMDB-41844, PDB-8u2b: EMDB-42136, PDB-8ucr: EMDB-42163, PDB-8uej: |
Chemicals | ChemComp-CA: |
Source |
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Keywords | PROTEIN FIBRIL / Complex / RECOMBINATION / RNA phage / VIRUS / ssRNA phage |