Crystal structure of the long-chain fatty acid transporter FadL - PubMed (original) (raw)
. 2004 Jun 4;304(5676):1506-9.
doi: 10.1126/science.1097524.
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- PMID: 15178802
- DOI: 10.1126/science.1097524
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Crystal structure of the long-chain fatty acid transporter FadL
Bert van den Berg et al. Science. 2004.
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Abstract
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.
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