Site-directed mutagenesis reveals the importance of conserved charged residues for the transport activity of the PheP permease of Escherichia coli.
Site-directed mutagenesis has been used to identify a number of charged residues essential for the transport activity of the PheP protein. These residues are highly conserved in the cluster of amino acid transporters. However, some other conserved residues and a number of aromatic residues have been shown not to be essential for transport activity.
Pi
J
J
Department of Microbiology, University of Melbourne, Parkville, Victoria, Australia.
Wookey
P J
PJ
Pittard
A J
AJ
D000595:Amino Acid Sequence; D026921:Amino Acid Transport Systems, Neutral; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001692:Biological Transport; D003062:Codon / Q000235:genetics; D017124:Conserved Sequence; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D026901:Membrane Transport Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010649:Phenylalanine / Q000378:metabolism; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D026921:Amino Acid Transport Systems, Neutral; D001426:Bacterial Proteins; D003062:Codon; D026901:Membrane Transport Proteins; D011994:Recombinant Proteins; C069320:phenylalanine-specific permease, E coli; D010649:Phenylalanine