1t1l: Difference between revisions
New page: left|200px<br /><applet load="1t1l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t1l, resolution 2.80Å" /> '''Crystal structure of... |
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[[Image:1t1l.jpg|left|200px]]<br /><applet load="1t1l" size=" | [[Image:1t1l.jpg|left|200px]]<br /><applet load="1t1l" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1t1l, resolution 2.80Å" /> | caption="1t1l, resolution 2.80Å" /> | ||
'''Crystal structure of the long-chain fatty acid transporter FadL'''<br /> | '''Crystal structure of the long-chain fatty acid transporter FadL'''<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== | ||
1T1L 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 LDA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1T1L 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=LDA:'>LDA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1L 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: LDA]] | [[Category: LDA]] | ||
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
[[Category: hatch domain]] | [[Category: hatch domain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:53 2008'' | ||
Revision as of 13:08, 21 February 2008
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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 with LDA as ligand. 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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