3pf1

E. coli FadL Asp348Ala mutant

spinqualitylabelsall models 3pf1, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pf1 is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: C8E, LDA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FADL_ECOLI Involved in translocation of long-chain fatty acids across the outer membrane. It is a receptor for the bacteriophage T2. FadL may form a specific channel. Publication Abstract from PubMed 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 beta-barrel membrane protein is a prerequisite for channel formation. Ligand-gated diffusion across the bacterial outer membrane.,Lepore BW, Indic M, Pham H, Hearn EM, Patel DR, van den Berg B Proc Natl Acad Sci U S A. 2011 May 18. PMID:21593406 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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