Crystal structure of the long-chain fatty acid transporter FadL

Bert Van Den Berg, Paul N. Black, William M. Clemons, Tom A. Rapoport

Research output: Contribution to journalArticlepeer-review

183 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1506-1509
Number of pages4
Issue number5676
StatePublished - Jun 4 2004
Externally publishedYes

ASJC Scopus subject areas

  • General


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