Structural highlights
Function
[FADL_ECOLI] Involved in translocation of long-chain fatty acids across the outer membrane. It is a receptor for the bacteriophage T2. FadL may form a specific channel.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The mechanisms by which hydrophobic molecules, such as long-chain fatty acids, enter cells are poorly understood. In Gram-negative bacteria, the lipopolysaccharide layer in the outer membrane is an efficient barrier for fatty acids and aromatic hydrocarbons destined for biodegradation. We report crystal structures of the long-chain fatty acid transporter FadL from Escherichia coli at 2.6 and 2.8 angstrom resolution. FadL forms a 14-stranded beta barrel that is occluded by a central hatch domain. The structures suggest that hydrophobic compounds bind to multiple sites in FadL and use a transport mechanism that involves spontaneous conformational changes in the hatch.
Crystal structure of the long-chain fatty acid transporter FadL.,van den Berg B, Black PN, Clemons WM Jr, Rapoport TA Science. 2004 Jun 4;304(5676):1506-9. PMID:15178802[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van den Berg B, Black PN, Clemons WM Jr, Rapoport TA. Crystal structure of the long-chain fatty acid transporter FadL. Science. 2004 Jun 4;304(5676):1506-9. PMID:15178802 doi:10.1126/science.1097524
