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1t1l

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[[Image:1t1l.jpg|left|200px]]
[[Image:1t1l.jpg|left|200px]]
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{{Structure
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|PDB= 1t1l |SIZE=350|CAPTION= <scene name='initialview01'>1t1l</scene>, resolution 2.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1t1l", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>
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|GENE= FADL, TTR, B2344 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1t1l| PDB=1t1l | SCENE= }}
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|RELATEDENTRY=[[1t16|1T16]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t1l OCA], [http://www.ebi.ac.uk/pdbsum/1t1l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t1l RCSB]</span>
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'''Crystal structure of the long-chain fatty acid transporter FadL'''
'''Crystal structure of the long-chain fatty acid transporter FadL'''
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[[Category: Jr., W M.Clemons.]]
[[Category: Jr., W M.Clemons.]]
[[Category: Rapoport, T A.]]
[[Category: Rapoport, T A.]]
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[[Category: beta-barrel]]
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[[Category: Beta-barrel]]
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[[Category: hatch domain]]
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[[Category: Hatch domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:23:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:57 2008''
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Revision as of 06:23, 3 May 2008

Image:1t1l.jpg

Template:STRUCTURE 1t1l

Crystal structure of the long-chain fatty acid transporter FadL


Overview

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.

About this Structure

1T1L is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 09:23:38 2008

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