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

Autor: Albert Guskov, Mikhail S. Gelfand, Pavlo Stehantsev, Natalia O. Dranenko, Artem Stetsenko
Přispěvatelé: X-ray Crystallography
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Zdroj: International Journal of Biological Macromolecules, 184, 760-767. ELSEVIER SCIENCE BV
ISSN: 0141-8130
DOI: 10.1016/j.ijbiomac.2021.06.130
Popis: 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 Zn2+, Mg2+, Cd2+, Ni2+ and Co2+ 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.
Databáze: OpenAIRE