PMID:15292155

Citation	Bertrand, J, Altendorf, K and Bramkamp, M (2004) Amino acid substitutions in putative selectivity filter regions III and IV in KdpA alter ion selectivity of the KdpFABC complex from Escherichia coli. J. Bacteriol. 186:5519-22
Abstract	When grown under conditions of potassium limitation or high osmolality, Escherichia coli synthesizes the K(+)-translocating KdpFABC complex. The KdpA subunit, which has sequence homology to potassium channels of the KcsA type, has been shown to be important for potassium binding and transport. Replacement of the glycine residues in KdpA at positions 345 and 470, members of putative selectivity filter regions III and IV, alters the ion selectivity of the KdpFABC complex.
Links	PubMed PMC490938 Online version:10.1128/JB.186.16.5519-5522.2004
Keywords	Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Amino Acid Substitution; Cation Transport Proteins/chemistry; Cation Transport Proteins/genetics; Cation Transport Proteins/metabolism; Cations, Monovalent/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Genes, Bacterial; Mutagenesis, Site-Directed; Mutation, Missense; Potassium/metabolism; Protein Structure, Tertiary; Protein Subunits/genetics; Protein Subunits/metabolism; Substrate Specificity
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