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TitleStructural and biochemical characterization of a novel ZntB (CmaX) transporter protein from Pseudomonas aeruginosa.
Journal, issue, pagesInt J Biol Macromol, Vol. 184, Page 760-767, Year 2021
Publish dateAug 1, 2021
AuthorsArtem Stetsenko / Pavlo Stehantsev / Natalia O Dranenko / Mikhail S Gelfand / Albert Guskov /
PubMed AbstractThe 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, ...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, Mg, Cd, Ni and Co 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.
External linksInt J Biol Macromol / PubMed:34175341
MethodsEM (single particle)
Resolution3.03 Å
Structure data

12321

7nh9

EMDB-12321, PDB-7nh9:
structure of the full-length CmaX protein
Method: EM (single particle) / Resolution: 3.03 Å

Source
  • Pseudomonas aeruginosa (bacteria)
  • pseudomonas aeruginosa (strain atcc 15692 / dsm 22644 / cip 104116 / jcm 14847 / lmg 12228 / 1c / prs 101 / pao1) (bacteria)
KeywordsTRANSPORT PROTEIN / divalent transport / zinc transporter / CorA family / membrane protein

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