A topological model for the general aromatic amino acid permease, AroP, of Escherichia coli.

Abstract:

:The general aromatic amino acid permease, AroP, of Escherichia coli is responsible for the active transport of phenylalanine, tyrosine, and tryptophan. A proposed topological model for the AroP permease, consisting of 12 hydrophobic transmembrane spans connected by hydrophilic loops, is very similar to that of the closely related phenylalanine-specific permease. The validity of this model and its similarity to that of the PheP permease were investigated by studying fusion proteins of AroP permease and alkaline phosphatase. Based on the results obtained from the AroP-alkaline phosphatase sandwich fusions, we have significantly revised the proposed topological model for AroP in two regions. In this modified AroP topological model, the three charged residues E151, E153, and K160 are repositioned within the membrane in span 5. These three residues are conserved in a large family of amino acid transport proteins, and site-directed mutagenesis identifies them as being essential for transport activity. It is postulated that these residues together with E110 in transmembrane span 3 may be involved in a proton relay system.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Cosgriff AJ,Pittard AJ

doi

10.1128/jb.179.10.3317-3323.1997

subject

Has Abstract

pub_date

1997-05-01 00:00:00

pages

3317-23

issue

10

eissn

0021-9193

issn

1098-5530

journal_volume

179

pub_type

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