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Science 2 June 2006:
Vol. 312. no. 5778, pp. 1396 - 1399
DOI: 10.1126/science.1127694
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Reports

Outer Membrane Active Transport: Structure of the BtuB:TonB Complex

David D. Shultis,1 Michael D. Purdy,1 Christian N. Banchs,2 Michael C. Wiener1,2*

In Gram-negative bacteria, the import of essential micronutrients across the outer membrane requires a transporter, an electrochemical gradient of protons across the inner membrane, and an inner membrane protein complex (ExbB, ExbD, TonB) that couples the proton-motive force to the outer membrane transporter. The inner membrane protein TonB binds directly to a conserved region, called the Ton-box, of the transporter. We solved the structure of the cobalamin transporter BtuB in complex with the C-terminal domain of TonB. In contrast to its conformations in the absence of TonB, the Ton-box forms a ß strand that is recruited to the existing ß sheet of TonB, which is consistent with a mechanical pulling model of transport.

1 Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA.
2 Interdisciplinary Graduate Program in Biophysics, University of Virginia, Charlottesville, VA 22908, USA.

* To whom correspondence should be addressed. E-mail: mwiener{at}virginia.edu

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