The Potassium Binding Protein Kbp Is a Cytoplasmic Potassium Sensor

Structure. 2016 May 3;24(5):741-749. doi: 10.1016/j.str.2016.03.017. Epub 2016 Apr 21.

Abstract

Escherichia coli possesses a number of specific K(+) influx and efflux systems that maintain an appropriate intracellular K(+) concentration. Although regulatory mechanisms have been identified for a number of these transport systems, the exact mechanism through which K(+) concentration is sensed in the cell remains unknown. In this work we show that Kbp (K(+) binding protein, formerly YgaU), a soluble 16-kDa cytoplasmic protein from Escherichia coli, is a highly specific K(+) binding protein and is required for normal growth in the presence of high levels of external K(+). Kbp binds a single potassium ion with high specificity over Na(+) and other metal ions found in biological systems, although, in common with K(+) transporters, it also binds Rb(+) and Cs(+). Dissection of the K(+) binding determinants of Kbp suggests a mechanism through which Kbp is able to sense changes in K(+) concentration over the relevant range of intracellular K(+) concentrations.

MeSH terms

  • Binding Sites
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism
  • Molecular Docking Simulation
  • Molecular Dynamics Simulation
  • Potassium / metabolism*
  • Protein Binding
  • Sodium / metabolism

Substances

  • Escherichia coli Proteins
  • YgaU protein, E coli
  • Sodium
  • Potassium