'The multiple transferable resistance (mTR) pump from Neisseria gonorrhoeae MtrCDE multidrug pump is assembled from the inner and outer membrane proteins MtrD and MtrE and the periplasmic membrane fusion protein MtrC. Previously we established that while there is a weak interaction of MtrD and MtrE, MtrC binds with relatively high ... More
Resurrection of the flagellar rotary motor near zero load.
AuthorsYuan J, Berg HC
JournalProc Natl Acad Sci U S A
PubMed ID18202173
Flagellated bacteria, such as Escherichia coli, are propelled by helical flagellar filaments, each driven at its base by a reversible rotary motor, powered by a transmembrane proton flux. Torque is generated by the interaction of stator proteins, MotA and MotB, with a rotor protein FliG. The physiology of the motor ... More
A periplasmic coiled-coil interface underlying TolC recruitment and the assembly of bacterial drug efflux pumps.
AuthorsLobedanz S, Bokma E, Symmons MF, Koronakis E, Hughes C, Koronakis V
JournalProc Natl Acad Sci U S A
PubMed ID17360572
Bacteria such as Escherichia coli and Pseudomonas aeruginosa expel antibiotics and other inhibitors via tripartite multidrug efflux pumps spanning the inner and outer membranes and the intervening periplasmic space. A key event in pump assembly is the recruitment of an outer membrane-anchored TolC exit duct by the adaptor protein of ... More
The assembled structure of a complete tripartite bacterial multidrug efflux pump.
AuthorsSymmons MF, Bokma E, Koronakis E, Hughes C, Koronakis V
JournalProc Natl Acad Sci U S A
PubMed ID19342493
Bacteria like Escherichia coli and Pseudomonas aeruginosa expel drugs via tripartite multidrug efflux pumps spanning both inner and outer membranes and the intervening periplasm. In these pumps a periplasmic adaptor protein connects a substrate-binding inner membrane transporter to an outer membrane-anchored TolC-type exit duct. High-resolution structures of all 3 components ... More