1T16

Crystal structure of the bacterial fatty acid transporter FadL from Escherichia coli

1T16 の概要

• エントリーDOI: 10.2210/pdb1t16/pdb
• 関連するPDBエントリー: 1T1L
• 分子名称: Long-chain fatty acid transport protein, COPPER (II) ION, LAURYL DIMETHYLAMINE-N-OXIDE, ... (5 entities in total)
• 機能のキーワード: beta-barrel, lipid transport
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P10384
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95752.19

構造登録者

van den Berg, B.,Black, P.N.,Clemons Jr., W.M.,Rapoport, T.A. (登録日: 2004-04-15, 公開日: 2004-06-15, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.6 Å)