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3pgr
From Proteopedia
(Difference between revisions)
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| - | + | ==Asp348Arg mutant of EcFadL== | |
| - | === | + | <StructureSection load='3pgr' size='340' side='right' caption='[[3pgr]], [[Resolution|resolution]] 2.60Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3pgr]] is a 1 chain structure with sequence from [http://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=3PGR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PGR 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></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t1l|1t1l]], [[1t16|1t16]], [[3pf1|3pf1]]</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 Escherichia coli K-12])</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=3pgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pgr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pgr RCSB], [http://www.ebi.ac.uk/pdbsum/3pgr PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:21593406</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
| - | [[Category: Berg, B van den | + | [[Category: Berg, B van den]] |
| - | [[Category: Hearn, E | + | [[Category: Hearn, E]] |
| - | [[Category: Indic, M | + | [[Category: Indic, M]] |
| - | [[Category: Lepore, B W | + | [[Category: Lepore, B W]] |
| - | [[Category: Patel, D | + | [[Category: Patel, D]] |
| - | [[Category: Pham, H | + | [[Category: Pham, H]] |
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Lipid transport]] | [[Category: Lipid transport]] | ||
[[Category: Outer membrane]] | [[Category: Outer membrane]] | ||
Revision as of 07:22, 19 December 2014
Asp348Arg mutant of EcFadL
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