7nh9

structure of the full-length CmaX protein

spinqualitylabelsall models 7nh9, resolution 3.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.03Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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