9VF4
CryoEM structure of phospholipid-independent cyclised RP4 pilus
Summary for 9VF4
| Entry DOI | 10.2210/pdb9vf4/pdb |
| EMDB information | 65024 |
| Descriptor | TrbC/VIRB2 family protein (1 entity in total) |
| Functional Keywords | pilus, conjugation, antibiotic, protein fibril |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 8139.47 |
| Authors | Ishimoto, N.,Beis, K. (deposition date: 2025-06-10, release date: 2026-05-27, Last modification date: 2026-07-01) |
| Primary citation | Ishimoto, N.,He, S.,Bogdanov, M.,Smith, T.K.,Frankel, G.,Beis, K. Phospholipid-independent biogenesis and function of the RP4 conjugation pilus. Nat Commun, 2026 Cited by PubMed Abstract: Bacterial conjugation, the process of horizontal gene transfer between bacteria, is initiated by mating pair formation (MPF) via a conjugative pilus. Conjugation of the IncP RP4 plasmid is mediated by short mating pili. Here, we report the cryo-EM structure of the RP4 pilus at 2.74 Å resolution. Uniquely, both the structural and quantitative mass spectral analyses revealed that the cyclic TrbC pilin subunit is not lipidated. Consistently, an E. coli pgsA mutant lacking phosphatidylglycerol (PG) can serve as a donor of RP4 but not of F- (pKpQIL), H- (R27) or W- (R388) pili, whose biogenesis and DNA transfer is PG-dependent. RP4 is the first example of a lipid-independent functional mating pilus. This discovery suggests that an amphipathic lipid moiety is not universally essential for the biogenesis of conjugative pili and MPF, providing an alternative model for their assembly and function. These data expand our understanding of the diverse bacterial mechanisms employ to transfer genetic material. PubMed: 42310306DOI: 10.1038/s41467-026-74409-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.74 Å) |
Structure validation
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