2f1t
From Proteopedia
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|PDB= 2f1t |SIZE=350|CAPTION= <scene name='initialview01'>2f1t</scene>, resolution 3.0Å | |PDB= 2f1t |SIZE=350|CAPTION= <scene name='initialview01'>2f1t</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ompW ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ompW ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1t OCA], [http://www.ebi.ac.uk/pdbsum/2f1t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f1t RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Berg, B van den.]] | [[Category: Berg, B van den.]] | ||
| - | [[Category: C8E]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: LDA]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: outer membrane protein]] | [[Category: outer membrane protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:56:43 2008'' |
Revision as of 23:56, 30 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | ompW (Escherichia coli) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Outer membrane protein OmpW
Overview
Escherichia coli OmpW belongs to a family of small outer membrane proteins that are widespread in Gram-negative bacteria. Their functions are unknown, but recent data suggest that they may be involved in the protection of bacteria against various forms of environmental stress. To gain insight into the function of these proteins A we have determined the crystal structure of E. coli OmpW to 2.7-A resolution. The structure shows that OmpW forms an 8-stranded beta-barrel with a long and narrow hydrophobic channel that contains a bound n-dodecyl-N,N-dimethylamine-N-oxide detergent molecule. Single channel conductance experiments show that OmpW functions as an ion channel in planar lipid bilayers. The channel activity can be blocked by the addition of n-dodecyl-N,N-dimethylamine-N-oxide. Taken together, the data suggest that members of the OmpW family could be involved in the transport of small hydrophobic molecules across the bacterial outer membrane.
About this Structure
2F1T is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The outer membrane protein OmpW forms an eight-stranded beta-barrel with a hydrophobic channel., Hong H, Patel DR, Tamm LK, van den Berg B, J Biol Chem. 2006 Mar 17;281(11):7568-77. Epub 2006 Jan 12. PMID:16414958
Page seeded by OCA on Mon Mar 31 02:56:43 2008
