2f1v | pdb_00002f1v
Outer membrane protein OmpW
Structural highlights
FunctionOMPW_ECOLI Acts as a receptor for colicin S4.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEscherichia 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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