PMID:14563856

Citation	Dogovski, C, Pi, J and Pittard, AJ (2003) Putative interhelical interactions within the PheP protein revealed by second-site suppressor analysis. J. Bacteriol. 185:6225-32
Abstract	Highly conserved glycine residues within span I and span II of the phenylalanine and tyrosine transporter PheP were shown to be important for the function of the wild-type protein. Replacement by amino acids with increasing side chain volume led to progressive loss of transport activity. Second-site suppression studies performed with a number of the primary mutants revealed a tight packing arrangement between spans I and II that is important for function and an additional interaction between spans I and III. We also postulate that a third motif, GXXIG, present in span I and highly conserved within different members of the amino acid-polyamine-organocation family, may function as a dimerization motif. Surprisingly, other highly conserved residues, such as Y60 and L41, could be replaced by various residues with no apparent loss of activity.
Links	PubMed PMC219386
Keywords	Amino Acid Sequence; Amino Acid Transport Systems, Neutral/genetics; Amino Acid Transport Systems, Neutral/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Dimerization; Escherichia coli/enzymology; Escherichia coli/genetics; Glycine/metabolism; Molecular Sequence Data; Mutagenesis, Insertional; Nucleic Acid Conformation; Signal Transduction
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