1t16
From Proteopedia
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|PDB= 1t16 |SIZE=350|CAPTION= <scene name='initialview01'>1t16</scene>, resolution 2.60Å | |PDB= 1t16 |SIZE=350|CAPTION= <scene name='initialview01'>1t16</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA | + | |LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= FADL, TTR, B2344 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= FADL, TTR, B2344 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1t1l|1T1L]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t16 OCA], [http://www.ebi.ac.uk/pdbsum/1t16 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t16 RCSB]</span> | ||
}} | }} | ||
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[[Category: Jr., W M.Clemons.]] | [[Category: Jr., W M.Clemons.]] | ||
[[Category: Rapoport, T A.]] | [[Category: Rapoport, T A.]] | ||
- | [[Category: C8E]] | ||
- | [[Category: CU]] | ||
- | [[Category: LDA]] | ||
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:44 2008'' |
Revision as of 20:49, 30 March 2008
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, resolution 2.60Å | |||||||
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Ligands: | , , | ||||||
Gene: | FADL, TTR, B2344 (Escherichia coli) | ||||||
Related: | 1T1L
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of the bacterial fatty acid transporter FadL from Escherichia coli
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
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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