1T1L

Crystal structure of the long-chain fatty acid transporter FadL

Summary for 1T1L

• Entry DOI: 10.2210/pdb1t1l/pdb
• Related: 1T16
• Descriptor: Long-chain fatty acid transport protein, LAURYL DIMETHYLAMINE-N-OXIDE (3 entities in total)
• Functional Keywords: beta-barrel, hatch domain, lipid transport
• Biological source: Escherichia coli
• Cellular location: Cell outer membrane; Multi-pass membrane protein: P10384
• Total number of polymer chains: 2
• Total formula weight: 93992.80

Authors

van den Berg, B.,Black, P.N.,Clemons Jr., W.M.,Rapoport, T.A. (deposition date: 2004-04-16, release date: 2004-06-15, Last modification date: 2024-02-14)

Primary citation

van den Berg, B.,Black, P.N.,Clemons Jr., W.M.,Rapoport, T.A.
Crystal structure of the long-chain fatty acid transporter FadL.
Science, 304:1506-1509, 2004

PubMed 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.

PubMed: 15178802
DOI: 10.1126/science.1097524

Experimental method

X-RAY DIFFRACTION (2.8 Å)