Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 15, Issue 4, Pages 401-407Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2005.06.003
Keywords
-
Categories
Ask authors/readers for more resources
The FadL family of proteins is responsible for the transport of hydrophobic compounds across the bacterial outer membrane. Two crystal structures of FadL, the long-chain fatty acid transporter from Escherichia coli, were recently determined, showing a novel fold characterized by the combination of a 14-stranded beta barrel and a 'hatch' domain that plugs the barrel. Both crystal forms have several bound detergent molecules in the interior of the protein. This, together with differences between the N-terminal conformations of the FadL structures, has led to the proposal of a transport model that is distinct from those of all other known outer membrane transporters. According to this model, the transport of hydrophobic substrates across the outer membrane, as mediated by FadL family members, is based on diffusion, coupled to spontaneous conformational changes in the hatch domain.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available