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Crystal Structure of the Long-Chain Fatty Acid Transporter FadL
Bert van den Berg, Paul N. Black, William M. Clemons Jr. and Tom A. Rapoport
New Series, Vol. 304, No. 5676 (Jun. 4, 2004), pp. 1506-1509
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/3837089
Page Count: 4
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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 β 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.
Science © 2004 American Association for the Advancement of Science