3q7k

Publication Abstract from PubMed

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.

pH-dependent gating in a FocA formate channel.,Lu W, Du J, Wacker T, Gerbig-Smentek E, Andrade SL, Einsle O Science. 2011 Apr 15;332(6027):352-4. PMID:21493860^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.