1t16: Difference between revisions

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[[Image:1t16.gif|left|200px]]
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[[Image:1t16.png|left|200px]]


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{{STRUCTURE_1t16|  PDB=1t16  |  SCENE=  }}  
{{STRUCTURE_1t16|  PDB=1t16  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_15178802}}


==About this Structure==
==About this Structure==
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[[Category: Rapoport, T A.]]
[[Category: Rapoport, T A.]]
[[Category: Beta-barrel]]
[[Category: Beta-barrel]]
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Revision as of 19:34, 27 July 2008

File:1t16.png

Template:STRUCTURE 1t16

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

Template:ABSTRACT PUBMED 15178802

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

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