Modulation of the SecY channel permeability by pore mutations and trivalent cations.

Abstract excerpt

The SecY channel serves to transport proteins across the bacterial inner membrane. The closed channel is impermeable to small molecules by means of a plug domain and a hydrophobic pore, consisting of six conserved isoleucine residues. The substitution of these isoleucines by asparagine leads to the selective conductance of small monovalent anions, especially chloride. In this addendum, we show that replacement of...

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