1t16

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[[Image:1t16.gif|left|200px]]
[[Image:1t16.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1t16 |SIZE=350|CAPTION= <scene name='initialview01'>1t16</scene>, resolution 2.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1t16", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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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_1t16| PDB=1t16 | SCENE= }}
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|RELATEDENTRY=[[1t1l|1T1L]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t16 OCA], [http://www.ebi.ac.uk/pdbsum/1t16 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t16 RCSB]</span>
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}}
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'''Crystal structure of the bacterial fatty acid transporter FadL from Escherichia coli'''
'''Crystal structure of the bacterial fatty acid transporter FadL from Escherichia coli'''
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:22:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:44 2008''
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Revision as of 06:22, 3 May 2008

Image:1t16.gif

Template:STRUCTURE 1t16

Crystal structure of the bacterial fatty acid transporter FadL from Escherichia coli


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

1T16 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 09:22:41 2008

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