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1t1l

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{{STRUCTURE_1t1l| PDB=1t1l | SCENE= }}
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'''Crystal structure of the long-chain fatty acid transporter FadL'''
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===Crystal structure of the long-chain fatty acid transporter FadL===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 15178802 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15178802}}
==About this Structure==
==About this Structure==
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[[Category: Beta-barrel]]
[[Category: Beta-barrel]]
[[Category: Hatch domain]]
[[Category: Hatch domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:23:38 2008''
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Revision as of 06:32, 29 July 2008

Image:1t1l.png

Template:STRUCTURE 1t1l

Crystal structure of the long-chain fatty acid transporter FadL

Template:ABSTRACT PUBMED 15178802

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 Tue Jul 29 09:32:08 2008

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