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1t1l

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Current revision (08:35, 14 February 2024) (edit) (undo)
 
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<StructureSection load='1t1l' size='340' side='right'caption='[[1t1l]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1t1l' size='340' side='right'caption='[[1t1l]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[1t1l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1T1L FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<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>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t1l OCA], [https://pdbe.org/1t1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t1l RCSB], [https://www.ebi.ac.uk/pdbsum/1t1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t1l ProSAT]</span></td></tr>
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<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>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t1l ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t1l ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1t1l" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Berg, B van den]]
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[[Category: Black PN]]
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[[Category: Black, P N]]
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[[Category: Clemons Jr WM]]
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[[Category: Clemons, W M]]
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[[Category: Rapoport TA]]
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[[Category: Rapoport, T A]]
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[[Category: Van den Berg B]]
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[[Category: Beta-barrel]]
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[[Category: Hatch domain]]
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[[Category: Lipid transport]]
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Current revision

Crystal structure of the long-chain fatty acid transporter FadL

PDB ID 1t1l

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