3Q7K
Formate Channel FocA from Salmonella typhimurium
Summary for 3Q7K
Entry DOI | 10.2210/pdb3q7k/pdb |
Descriptor | Probable formate transporter, FORMIC ACID (3 entities in total) |
Functional Keywords | membrane protein, transport, cytoplasmic membrane, transport protein |
Biological source | Salmonella enterica subsp. enterica serovar Typhi |
Total number of polymer chains | 10 |
Total formula weight | 321216.38 |
Authors | Lue, W.,Du, J.,Wacker, T.,Gerbig-Smentek, E.,Andrade, S.L.A.,Einsle, O. (deposition date: 2011-01-05, release date: 2011-04-27, Last modification date: 2023-11-01) |
Primary citation | Lu, W.,Du, J.,Wacker, T.,Gerbig-Smentek, E.,Andrade, S.L.,Einsle, O. pH-dependent gating in a FocA formate channel Science, 332:352-354, 2011 Cited by PubMed 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. PubMed: 21493860DOI: 10.1126/science.1199098 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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