9TG4
Structure of the YbjP lipoprotein bound to the AcrABZ-TolC efflux pump
This is a non-PDB format compatible entry.
Summary for 9TG4
| Entry DOI | 10.2210/pdb9tg4/pdb |
| Related | 9QGY |
| EMDB information | 55890 |
| Descriptor | Outer membrane protein TolC, Multidrug efflux pump subunit AcrA, Multidrug efflux pump subunit AcrB, ... (6 entities in total) |
| Functional Keywords | multi-drug efflux pump, rnd transporter, macab-tolc, acrabz-tolc, type i secretion, lipoprotein, membrane protein assembly, membrane protein, transport protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 18 |
| Total formula weight | 822679.86 |
| Authors | Kaplan, E.,Harris, A.,Horne, J.,Petsolari, E.,Luisi, B. (deposition date: 2025-11-28, release date: 2026-04-08, Last modification date: 2026-10-07) |
| Primary citation | Horne, J.,Kaplan, E.,Jin, B.,Abbott, K.,Flores, V.,Petsolari, E.,Gradon, J.,Ntsogo, Y.,Harris, A.,Yu, D.,Zarkan, A.,Luisi, B.F. A lipoprotein partner for the Escherichia coli outer membrane protein TolC. Elife, 15:-, 2026 Cited by PubMed Abstract: The outer membrane protein TolC from belongs to an extensive superfamily whose members are found throughout the didermal, Gram-negative bacterial lineages. The protein serves as an activated exit duct in multi-drug efflux pumps and protein secretion machinery. Many TolC homologues bear a lipid modification on the N-terminus that embeds into the inner leaflet of the outer membrane and appears to have been a conserved feature; however, the moiety is absent entirely in the TolC. We have discovered that the lipoprotein YbjP interacts extensively with the periplasmic surface of TolC and its N-terminal lipid moiety is embedded in the membrane, mimicking the intramolecular and modification-membrane interactions seen in TolC homologues. Here, we present cryo-EM structures of the MacA-MacB-TolC and AcrA-AcrB-TolC tripartite pumps complexed to YbjP. Although the association occurs spontaneously both in vitro and in vivo, the YbjP-TolC interaction is not required for efflux activity under standard laboratory conditions. YbjP may contribute to stabilising the orientation and distribution of TolC in the outer membrane, as well as the expression of transporters for tryptophan and cyclic peptide toxins. PubMed: 41984076DOI: 10.7554/eLife.110666 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.17 Å) |
Structure validation
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