3PF1

E. coli FadL Asp348Ala mutant

Summary for 3PF1

• Entry DOI: 10.2210/pdb3pf1/pdb
• Related: 1T16 1T1L 2R4O 2R89 2R8A
• Descriptor: Long-chain fatty acid transport protein, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, LAURYL DIMETHYLAMINE-N-OXIDE, ... (4 entities in total)
• Functional Keywords: outer membrane protein, oleate, oleic, beta barrel, 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: 95756.82

Authors

Vandenberg, B.,Lepore, B.W.,Hearn, E.M.,Indic, M.,Patel, D. (deposition date: 2010-10-27, release date: 2011-05-25, Last modification date: 2023-09-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)