Crystal Structure of the Long-Chain Fatty Acid Transporter FadL

@article{vandenBerg2004CrystalSO,
  title={Crystal Structure of the Long-Chain Fatty Acid Transporter FadL},
  author={Bert van den Berg and Paul N. Black and William M. Clemons and Tom A. Rapoport},
  journal={Science},
  year={2004},
  volume={304},
  pages={1506 - 1509}
}
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… 
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The FadL family: unusual transporters for unusual substrates
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Bacterial FadL constitutes a family of transmembrane proteins involved in the transport of long-chain fatty acids and the uptake of hydrophobic compounds including aromatic hydrocarbon destined for…
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By folding E. coli’s FadL homologs, the resulting putative pathways show important structural details of the transport protein, and the predicted transport mechanics of V. cholerae's uptake of long-chain fatty acids are studied to the atomistic level.
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Bacterial biodegradation of hydrocarbons, an important process for environmental remediation, requires the passage of hydrophobic substrates across the cell membrane. Here, we report crystal…
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Crystal structure of the monomeric porin OmpG.
The Outer Membrane Protein OmpW Forms an Eight-stranded β-Barrel with a Hydrophobic Channel*
TLDR
The crystal structure of E. coli OmpW is determined and it is suggested that members of the OMPW family could be involved in the transport of small hydrophobic molecules across the bacterial outer membrane.
Transmembrane passage of hydrophobic compounds through a protein channel wall
TLDR
The first example of a lateral diffusion mechanism for the uptake of hydrophobic substrates by the Escherichia coli outer membrane long-chain fatty acid transporter FadL is presented and has implications for combating bacterial infections and bioremediating xenobiotics in the environment.
Functional characterization of ExFadLO, an outer membrane protein required for exporting oxygenated long-chain fatty acids in Pseudomonas aeruginosa.
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