1t16
From Proteopedia
(New page: 200px<br /><applet load="1t16" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t16, resolution 2.60Å" /> '''Crystal structure of...) |
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| - | [[Image:1t16.gif|left|200px]]<br /><applet load="1t16" size=" | + | [[Image:1t16.gif|left|200px]]<br /><applet load="1t16" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t16, resolution 2.60Å" /> | caption="1t16, resolution 2.60Å" /> | ||
'''Crystal structure of the bacterial fatty acid transporter FadL from Escherichia coli'''<br /> | '''Crystal structure of the bacterial fatty acid transporter FadL from Escherichia coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The mechanisms by which hydrophobic molecules, such as long-chain fatty | + | 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== | ==About this Structure== | ||
| - | 1T16 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CU, LDA and C8E as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1T16 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=LDA:'>LDA</scene> and <scene name='pdbligand=C8E:'>C8E</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T16 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Berg, B | + | [[Category: Berg, B van den.]] |
| - | [[Category: Black, P | + | [[Category: Black, P N.]] |
| - | [[Category: Jr., W | + | [[Category: Jr., W M.Clemons.]] |
| - | [[Category: Rapoport, T | + | [[Category: Rapoport, T A.]] |
[[Category: C8E]] | [[Category: C8E]] | ||
[[Category: CU]] | [[Category: CU]] | ||
| Line 22: | Line 22: | ||
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:47 2008'' |
Revision as of 13:08, 21 February 2008
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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 with , and as ligands. 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 Thu Feb 21 15:08:47 2008
