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J. Biol. Chem., Vol. 281, Issue 11, 7568-7577, March 17, 2006

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The Outer Membrane Protein OmpW Forms an Eight-stranded -Barrel with a Hydrophobic Channel^*

Heedeok Hong, Dimki R. Patel, Lukas K. Tamm, and Bert van den Berg¹

From the Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908 and the Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605

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 Å we have determined the crystal structure of E. coli OmpW to 2.7-A resolution. The structure shows that OmpW forms an 8-stranded -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.

Received for publication, November 17, 2005 , and in revised form, January 10, 2006.

The atomic coordinates and structure factors (code 2F1T (trigonal) and 2F1V (orthorhombic OmpW)) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported in part by National Institutes of Health Grant GM051329 (to L. K. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by National Institutes of Health Grant GM074824 and a PEW scholarship. To whom correspondence should be addressed: 373 Plantation St., Worcester, MA 01605. Tel.: 508-856-1201; Fax: 508-856-4289; E-mail: bert.vandenberg{at}umassmed.edu.

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