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 |
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Přispěvatelé: | X-ray Crystallography |
Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
Models
Molecular Protein Conformation Amino Acid Motifs Cmax 02 engineering and technology medicine.disease_cause Biochemistry Divalent 03 medical and health sciences Bacterial Proteins Membrane proteins medicine Cloning Molecular Molecular Biology Escherichia coli Cation Transport Proteins 030304 developmental biology chemistry.chemical_classification 0303 health sciences biology Pseudomonas aeruginosa Magnesium transport Cryoelectron Microscopy Biological Transport General Medicine 021001 nanoscience & nanotechnology biology.organism_classification CorA proteins Transport protein Structural biology chemistry Membrane protein Protein Multimerization 0210 nano-technology Bacteria |
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 |
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