A team of 10 researchers, including seven from Utrecht University, have unravelled the mechanism behind the protein MraY. This protein, called phospho-MurNAC-pentapeptide translocase, plays an essential role in bacterial cell wall synthesis. According to the researchers’ publication in the 15 July issue of The Journal of Biological Chemistry (JBC), knowledge of how MraY works provides new insights that could be used to develop antibiotics.
Cell wall synthesis
MraY is an enzyme that occurs in the cell membranes of bacteria. This means that it functions as a catalyst in a specific chemical reaction, and in this case provides an important step in cell wall synthesis. The cell wall is a layer formed around a cell’s outer membrane. If MraY does not function correctly, then the bacteria cannot create a cell wall. This will eventually cause the bacteria to burst, as the weakened cell wall cannot hold against the difference in pressure inside the cell and outside. Human cells do not have cell walls, so MraY may be a good target for antibiotics.
Target for antibiotics
MraY is responsible for the first membrane-related step in cell wall synthesis. It binds a sugar molecule attached to a chain of five amino acids, which are the building blocks of proteins, to a special lipid anchor located on the surface of the cell membrane. The researchers studied this process in detail and found that one of the amino acids in MraY, histidine 289, plays an important role. This is a location in the protein that has not yet been used as a target for designing antibiotics.