3PF1

E. coli FadL Asp348Ala mutant

3PF1 の概要

• エントリーDOI: 10.2210/pdb3pf1/pdb
• 関連するPDBエントリー: 1T16 1T1L 2R4O 2R89 2R8A
• 分子名称: Long-chain fatty acid transport protein, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, LAURYL DIMETHYLAMINE-N-OXIDE, ... (4 entities in total)
• 機能のキーワード: outer membrane protein, oleate, oleic, 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: 95756.82

構造登録者

Vandenberg, B.,Lepore, B.W.,Hearn, E.M.,Indic, M.,Patel, D. (登録日: 2010-10-27, 公開日: 2011-05-25, 最終更新日: 2023-09-06)

主引用文献

Lepore, B.W.,Indic, M.,Pham, H.,Hearn, E.M.,Patel, D.R.,van den Berg, B.
From the Cover: Ligand-gated diffusion across the bacterial outer membrane.
Proc.Natl.Acad.Sci.USA, 108:10121-10126, 2011

PubMed Abstract: Ligand-gated channels, in which a substrate transport pathway is formed as a result of the binding of a small-molecule chemical messenger, constitute a diverse class of membrane proteins with important functions in prokaryotic and eukaryotic organisms. Despite their widespread nature, no ligand-gated channels have yet been found within the outer membrane (OM) of Gram-negative bacteria. Here we show, using in vivo transport assays, intrinsic tryptophan fluorescence and X-ray crystallography, that high-affinity (submicromolar) substrate binding to the OM long-chain fatty acid transporter FadL from Escherichia coli causes conformational changes in the N terminus that open up a channel for substrate diffusion. The OM long-chain fatty acid transporter FadL from E. coli is a unique paradigm for OM diffusion-driven transport, in which ligand gating within a β-barrel membrane protein is a prerequisite for channel formation.

PubMed: 21593406
DOI: 10.1073/pnas.1018532108

実験手法

X-RAY DIFFRACTION (2.7 Å)