Abstract
The outer membrane of Gram negative bacteria provides an effective barrier to diffusion of both hydrophilic and hydrophobic solutes. A number of recent X-ray studies have revealed the structures of outer membrane proteins, members of the FadL family, which are responsible for transport of hydrophobic solutes. These include: FadL from Escherichia coli (PDB id 1T16), TodX from Pseudomonas putida (PDB id 3BS0) and TbuX from Ralstonia pickettii (PDB id 3BRY). These proteins family has three significant structural features: 1) an N-terminal domain which blocks the pore otherwise formed by the transmembrane β-barrel; 2) a lateral opening formed by a kink in the β-barrel; and 3) a flexible L3 loop which seems to act as entry access point into the β-barrel.
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