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M704260200v1
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Papers In Press, published online ahead of print October 10, 2007
J. Biol. Chem, 10.1074/jbc.M704260200
Submitted on May 23, 2007
Revised on October 9, 2007
Accepted on October 10, 2007

Probing the structure of the dimeric KtrB membrane protein

Ronald A. Albright, Kyu Joh, and Joao H. Morais-Cabral

Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520

Corresponding Author: joao.cabral{at}yale.edu

The KtrAB ion transporter is a complex of two proteins, KtrB and KtrA. The integral membrane protein KtrB is expected to adopt the structural architecture typified by the pore domain of potassium channels. Here we show that homo-dimerization of KtrB proteins is most likely a general property of this family of transporters. Using cysteine mutants and bifunctional cross-linkers we define regions of the Bacillus subtilis KtrB molecule that are close to the molecular 2-fold axis and to the dimer interface. Fitting of the cross-linking data to a potassium channel-like model suggests structural similarities between potassium channels and KtrB proteins in the extracellular half of the molecule and differences in the cytoplasmic regions.


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[Abstract] [Full Text] [PDF]


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