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

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 tr...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 2006-06, Vol.312 (5778), p.1396-1399
Hauptverfasser: Shultis, David D, Purdy, Michael D, Banchs, Christian N, Wiener, Michael C
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1127694