2GSK

Outer membrane active transport: structure of the BtuB:TonB complex

(2006) Science 312: 1396-1399

• PubMed: 16741124 Search on PubMed
• DOI: https://doi.org/10.1126/science.1127694
• Primary Citation of Related Structures:  
  2GSK


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

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Organizational Affiliation: 

Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA.