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Science 4 June 2004:
Vol. 304. no. 5676, pp. 1506 - 1509
DOI: 10.1126/science.1097524
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Reports

Crystal Structure of the Long-Chain Fatty Acid Transporter FadL

Bert van den Berg,1* Paul N. Black,2 William M. Clemons, Jr.,1 Tom A. Rapoport1

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 ß 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.

1 Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
2 Center for Metabolic Disease, The Ordway Research Institute, 150 New Scotland Avenue, Albany, NY 12208, USA.

* To whom correspondence should be addressed. E-mail: lvandenberg{at}hms.harvard.edu

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