8U2B
Cryo-EM structure of C.crescentus bNY30a pilus complex
Summary for 8U2B
| Entry DOI | 10.2210/pdb8u2b/pdb |
| EMDB information | 41844 |
| Descriptor | Flp family type IVb pilin (1 entity in total) |
| Functional Keywords | complex, protein fibril |
| Biological source | Caulobacter vibrioides |
| Total number of polymer chains | 37 |
| Total formula weight | 162028.18 |
| Authors | |
| Primary citation | Wang, Y.,Theodore, M.,Xing, Z.,Narsaria, U.,Yu, Z.,Zeng, L.,Zhang, J. Structural mechanisms of Tad pilus assembly and its interaction with an RNA virus. Sci Adv, 10:eadl4450-eadl4450, 2024 Cited by 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 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. PubMed: 38701202DOI: 10.1126/sciadv.adl4450 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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