Once a strain of bacteria has built up resistance to an antibiotic, a new antibiotic with a different mechanism is our next move in the arms race against pathogens such as tuberculosis. To this end, Eddy Arnold and Richard Ebright of Rutgers University in Piscataway, New Jersey, and their colleagues have found a new point of attack on an already popular target, bacterial RNA polymerase. This enzyme makes a good target because it is essential for making proteins from RNA and is highly conserved across bacteria.
The new target is at the hinge of a dynamic region of the enzyme that exposes or hides its active site. The researchers show that three natural products, myxopyronin, corallopyronin and ripostatin, all compounds certain bacteria use against one another, bind at the hinge and shut down RNA polymerase activity, crippling the bacterium.
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Drug design: Hitting the hinge. Nature 455, 1011 (2008). https://doi.org/10.1038/4551011d
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DOI: https://doi.org/10.1038/4551011d
