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pH-Dependent Gating in a FocA Formate Channel

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Science  15 Apr 2011:
Vol. 332, Issue 6027, pp. 352-354
DOI: 10.1126/science.1199098

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Abstract

The formate transporter FocA was described to switch its mode of operation from a passive export channel at high external pH to a secondary active formate/H+ importer at low pH. The crystal structure of Salmonella typhimurium FocA at pH 4.0 shows that this switch involves a major rearrangement of the amino termini of individual protomers in the pentameric channel. The amino-terminal helices open or block transport in a concerted, cooperative action that indicates how FocA is gated in a pH-dependent way. Electrophysiological studies show that the protein acts as a specific formate channel at pH 7.0 and that it closes upon a shift of pH to 5.1.

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