Structural and biochemical characterization of a novel ZntB (CmaX) transporter protein from Pseudomonas aeruginosa

The 2-TM-GxN family of membrane proteins is widespread in prokaryotes and plays an important role transport divalent cations. canonical signature motif, which also a selectivity filter, has composition Gly-Met-Asn. Some members though deviate from this composition, however no data are available as to whether any functional implications. Here we report the structural analysis CmaX protein pathogenic Pseudomonas aeruginosa bacterium, Gly-Ile-Asn motif. readily transports Zn2+, Mg2+, Cd2+, Ni2+ Co2+ ions, but it does not utilize proton-symport ZntB Escherichia coli. Together with bioinformatics analysis, our suggest that deviations motif do reveal changes substrate or easily alter course evolution.