6VEJ

TriABC transporter from Pseudomonas aeruginosa

Summary for 6VEJ

• Entry DOI: 10.2210/pdb6vej/pdb
• EMDB information: 21361 21362 21363
• Descriptor: Probable Resistance-Nodulation-Cell Division (RND) efflux transporter, Probable Resistance-Nodulation-Cell Division (RND) efflux membrane fusion protein,Probable Resistance-Nodulation-Cell Division (RND) efflux membrane fusion protein, DODECYL-ALPHA-D-MALTOSIDE, ... (5 entities in total)
• Functional Keywords: rnd transporter, pseudomonas aeruginosa, transmembrane, triabc, tric, pmf, cryoem, transport protein
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 6
• Total formula weight: 565186.26

Authors

Sygusch, J.,Fabre, L.,Rouiller, I.,Bhattacharyya, S. (deposition date: 2020-01-02, release date: 2020-09-30, Last modification date: 2024-10-23)

Primary citation

Fabre, L.,Ntreh, A.T.,Yazidi, A.,Leus, I.V.,Weeks, J.W.,Bhattacharyya, S.,Ruickoldt, J.,Rouiller, I.,Zgurskaya, H.I.,Sygusch, J.
A "Drug Sweeping" State of the TriABC Triclosan Efflux Pump from Pseudomonas aeruginosa.
Structure, 29:261-, 2021

PubMed Abstract: The structure of the TriABC inner membrane component of the triclosan/SDS-specific efflux pump from Pseudomonas aeruginosa was determined by cryoelectron microscopy to 4.5 Å resolution. The complete structure of the inner membrane transporter TriC of the resistance-nodulation-division (RND) superfamily was solved, including a partial structure of the fused periplasmic membrane fusion subunits, TriA and TriB. The substrate-free conformation of TriABC represents an intermediate step in efflux complex assembly before the engagement of the outer membrane channel. Structural analysis identified a tunnel network whose constriction impedes substrate efflux, indicating inhibition of TriABC in the unengaged state. Blind docking studies revealed binding to TriC at the same loci by substrates and bulkier non-substrates. Together with functional analyses, we propose that selective substrate translocation involves conformational gating at the tunnel narrowing that, together with conformational ordering of TriA and TriB, creates an engaged state capable of mediating substrate efflux.

PubMed: 32966762
DOI: 10.1016/j.str.2020.09.001

Experimental method

ELECTRON MICROSCOPY (4.5 Å)