9X0X
Pseudomonas aeruginosa (PAO1) Outer membrane PilQ (Secretin) with SlkB in C14 symmetry
This is a non-PDB format compatible entry.
Summary for 9X0X
| Entry DOI | 10.2210/pdb9x0x/pdb |
| EMDB information | 66448 |
| Descriptor | Fimbrial assembly protein PilQ, Multidrug transporter, PHOSPHATIDYLETHANOLAMINE (3 entities in total) |
| Functional Keywords | type iv pili, secretin, plug, outer membrane, permeability barrier, antibiotics, drug resistance, transport protein |
| Biological source | Pseudomonas aeruginosa PAO1 More |
| Total number of polymer chains | 28 |
| Total formula weight | 1257158.07 |
| Authors | |
| Primary citation | Kwon, O.H.,Lee, Y.,Ryu, B.,Sher, J.W.,Park, S.,Lauber, F.,Kim, B.O.,Yoo, Y.,Cho, S.H.,Choe, D.,Cho, Y.H.,Collet, J.F.,Ohi, M.D.,Bernhardt, T.G.,Chung, J.M.,Cho, H. Secretin-interacting plug proteins prevent antibiotic influx during type IV pilus assembly in Pseudomonas aeruginosa. Nat Commun, 2026 Cited by PubMed Abstract: Type IV pili (T4P) are important virulence factors that mediate host attachment and other pathogenic functions. In Gram-negative bacteria, T4P are assembled from pilin subunits at the inner membrane (IM) and extend through the outer membrane (OM) via secretin channels. Although essential for T4P function, secretin complexes can impair the OM permeability barrier, potentially allowing entry of toxic compounds. The mechanisms that prevent such influx remain poorly understood. Here, we identify SlkA and SlkB (PA5122 and PA5123) as periplasmic proteins that interact with the T4P secretin channel and block antibiotic influx. Our data indicate that these proteins function as physical plugs sealing the channel until the IM complex docks and pilus assembly begins. These findings demonstrate that Slk proteins and the IM complex function redundantly to maintain OM barrier integrity, and that their interaction with the secretin channel represents a promising target for antibiotic potentiation. PubMed: 42215499DOI: 10.1038/s41467-026-73864-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.45 Å) |
Structure validation
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