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| | ==E. coli FadL Asp348Ala mutant== | | ==E. coli FadL Asp348Ala mutant== |
| - | <StructureSection load='3pf1' size='340' side='right' caption='[[3pf1]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='3pf1' size='340' side='right'caption='[[3pf1]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pf1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PF1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PF1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pf1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PF1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t16|1t16]], [[1t1l|1t1l]], [[2r89|2r89]], [[2r8a|2r8a]], [[2r4o|2r4o]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2344, fadL, JW2341, ttr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pf1 OCA], [https://pdbe.org/3pf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pf1 RCSB], [https://www.ebi.ac.uk/pdbsum/3pf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pf1 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pf1 OCA], [http://pdbe.org/3pf1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pf1 RCSB], [http://www.ebi.ac.uk/pdbsum/3pf1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pf1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FADL_ECOLI 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. | + | [https://www.uniprot.org/uniprot/FADL_ECOLI 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Hearn, E M]] | + | [[Category: Large Structures]] |
| - | [[Category: Indic, M]] | + | [[Category: Hearn EM]] |
| - | [[Category: Lepore, B W]] | + | [[Category: Indic M]] |
| - | [[Category: Patel, D]] | + | [[Category: Lepore BW]] |
| - | [[Category: Vandenberg, B]] | + | [[Category: Patel D]] |
| - | [[Category: Beta barrel]]
| + | [[Category: Vandenberg B]] |
| - | [[Category: Lipid transport]]
| + | |
| - | [[Category: Oleate]]
| + | |
| - | [[Category: Oleic]]
| + | |
| - | [[Category: Outer membrane protein]]
| + | |
| Structural highlights
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[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
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