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8U2B

Cryo-EM structure of C.crescentus bNY30a pilus complex

Summary for 8U2B
Entry DOI10.2210/pdb8u2b/pdb
EMDB information41844
DescriptorFlp family type IVb pilin (1 entity in total)
Functional Keywordscomplex, protein fibril
Biological sourceCaulobacter vibrioides
Total number of polymer chains37
Total formula weight162028.18
Authors
Wang, Y.,Zhang, J. (deposition date: 2023-09-05, release date: 2024-05-15, Last modification date: 2024-07-17)
Primary citationWang, 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: 38701202
DOI: 10.1126/sciadv.adl4450
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.8 Å)
Structure validation

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