A team has found a way to make the bacterial enzyme histidine kinase water-soluble, which could make it possible to rapidly screen potential antibiotics that might interfere with its functions.
A bacterial enzyme called histidine kinase is a promising target for new classes of antibiotics. However, it has been difficult to develop drugs that target this enzyme, because it is a"hydrophobic" protein that loses its structure once removed from its normal location in the cell membrane.
No existing antibiotics target histidine kinase, so drugs that disrupt these functions could represent a new class of antibiotics. Such drug candidates are badly needed to combat the growing problem of antibiotic resistance. In 2018, Zhang and his colleagues devised a simple way to convert these proteins into water-soluble versions, which maintain their structure in water. Their technique is known as the QTY code, for the letters that represent the hydrophilic amino acids that become incorporated into the proteins. Leucine becomes glutamine , isoleucine and valine become threonine , and phenylalanine becomes tyrosine .
The research team chose to focus on histidine kinase in part because of its potential as an antibiotic target. Currently most antibiotics work by damaging bacterial cell walls or interfering with the synthesis of ribosomes, the cell organelles that manufacture proteins. None of them target histidine kinase, an important bacterial protein that regulates processes such as antibiotic resistance and cell-to-cell communication.
They also found that if they only replaced the buried hydrophobic amino acids in the transmembrane segment, the protein would not retain its function. The hydrophobic amino acids have to be replaced throughout the transmembrane segment, which helps the molecule maintain the structural relationships it needs to function normally.
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