1t1l

<table><tr><td colspan='2'>[[1t1l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1T1L FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1t16|1t16]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FADL, TTR, B2344 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1t1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t1l OCA], [http://pdbe.org/1t1l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t1l RCSB], [http://www.ebi.ac.uk/pdbsum/1t1l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t1l ProSAT]</span></td></tr>

[[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.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The mechanisms by which hydrophobic molecules, such as long-chain fatty acids, enter cells are poorly understood. In Gram-negative bacteria, the lipopolysaccharide layer in the outer membrane is an efficient barrier for fatty acids and aromatic hydrocarbons destined for biodegradation. We report crystal structures of the long-chain fatty acid transporter FadL from Escherichia coli at 2.6 and 2.8 angstrom resolution. FadL forms a 14-stranded beta barrel that is occluded by a central hatch domain. The structures suggest that hydrophobic compounds bind to multiple sites in FadL and use a transport mechanism that involves spontaneous conformational changes in the hatch.

Crystal structure of the long-chain fatty acid transporter FadL.,van den Berg B, Black PN, Clemons WM Jr, Rapoport TA Science. 2004 Jun 4;304(5676):1506-9. PMID:15178802<ref>PMID:15178802</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1t1l" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Black, P N]]

[[Category: Clemons, W M]]

[[Category: Rapoport, T A]]

[[Category: Beta-barrel]]

[[Category: Lipid transport]]