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1t1l

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(New page: 200px<br /><applet load="1t1l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t1l, resolution 2.80&Aring;" /> '''Crystal structure of...)
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Revision as of 00:48, 21 November 2007

Image:1t1l.jpg

1t1l, resolution 2.80Å

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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

Page seeded by OCA on Wed Nov 21 02:55:16 2007

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