2R8A
Crystal structure of the long-chain fatty acid transporter FadL mutant delta N8
Summary for 2R8A
| Entry DOI | 10.2210/pdb2r8a/pdb |
| Related | 1T16 1T1L 2R4L 2R4M 2R4N 2R4O 2R4P 2R88 2R89 3DWN 3DWO |
| Descriptor | Long-chain fatty acid transport protein, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (2 entities in total) |
| Functional Keywords | beta barrel, outer membrane protein, lipid transport, phage recognition, transmembrane, transport, transport protein |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane; Multi-pass membrane protein: P10384 |
| Total number of polymer chains | 2 |
| Total formula weight | 92829.65 |
| Authors | Hearn, E.M.,Patel, D.R.,Lepore, B.W.,Indic, M.,van den Berg, B. (deposition date: 2007-09-10, release date: 2008-09-23, Last modification date: 2023-11-29) |
| 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 Cited by 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: 21593406DOI: 10.1073/pnas.1018532108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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