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

Author:

Shultis David D.12,Purdy Michael D.12,Banchs Christian N.12,Wiener Michael C.12

Affiliation:

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.

Abstract

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 β strand that is recruited to the existing β sheet of TonB, which is consistent with a mechanical pulling model of transport.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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