1t1l: Difference between revisions
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'''Crystal structure of the long-chain fatty acid transporter FadL''' | '''Crystal structure of the long-chain fatty acid transporter FadL''' | ||
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[[Category: Jr., W M.Clemons.]] | [[Category: Jr., W M.Clemons.]] | ||
[[Category: Rapoport, T A.]] | [[Category: Rapoport, T A.]] | ||
[[Category: | [[Category: Beta-barrel]] | ||
[[Category: | [[Category: Hatch domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:23:38 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 06:23, 3 May 2008
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 Page seeded by OCA on Sat May 3 09:23:38 2008
