7nh9

Publication Abstract from PubMed

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

Structural and biochemical characterization of a novel ZntB (CmaX) transporter protein from Pseudomonas aeruginosa.,Stetsenko A, Stehantsev P, Dranenko NO, Gelfand MS, Guskov A Int J Biol Macromol. 2021 Jun 24;184:760-767. doi:, 10.1016/j.ijbiomac.2021.06.130. PMID:34175341^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.