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1t1l

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|PDB= 1t1l |SIZE=350|CAPTION= <scene name='initialview01'>1t1l</scene>, resolution 2.80&Aring;
|PDB= 1t1l |SIZE=350|CAPTION= <scene name='initialview01'>1t1l</scene>, resolution 2.80&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=LDA:LAURYL DIMETHYLAMINE-N-OXIDE'>LDA</scene>
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|LIGAND= <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= FADL, TTR, B2344 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= FADL, TTR, B2344 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
 +
|DOMAIN=
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|RELATEDENTRY=[[1t16|1T16]]
 +
|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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[[Category: Jr., W M.Clemons.]]
[[Category: Jr., W M.Clemons.]]
[[Category: Rapoport, T A.]]
[[Category: Rapoport, T A.]]
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[[Category: LDA]]
 
[[Category: beta-barrel]]
[[Category: beta-barrel]]
[[Category: hatch domain]]
[[Category: hatch domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:12:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:57 2008''

Revision as of 20:49, 30 March 2008

Image:1t1l.jpg


PDB ID 1t1l

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands:
Gene: FADL, TTR, B2344 (Escherichia coli)
Related: 1T16


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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