Structural highlights
2r89 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Related: | 1t16, 1t1l, 2r4l, 2r4m, 2r4n, 2r4o, 2r4p, 2r88, 2r8a, 3dwo, 3dwn |
| Gene: | fadL, ttr (Escherichia coli) |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lepore BW, Indic M, Pham H, Hearn EM, Patel DR, van den Berg B. Ligand-gated diffusion across the bacterial outer membrane. Proc Natl Acad Sci U S A. 2011 May 18. PMID:21593406 doi:10.1073/pnas.1018532108
