Richard Ebright from Rutgers has a paper in Cell this week in which he and his team have unpicked the workings of a crucial bacterial enzyme that is a prime target for antibiotics. The enzyme in question is RNAP - RNA Polymerase, which is the linchpin in the process that helps to turn the cellular recipes written in the DNA in a bacterium into reality.
The work has revealed that the enzymes resembles a crab's claw and can open to latch onto a piece of DNA, and then close around the genetic material to read and translate it. The team have identified a region at the hinge of the molecular pincer that can be jammed by a novel antibiotic molecule they have developed called myxopronin.
Now they've discovered how the antibiotic works, it should be possible for the team to find other molecules like myxopronin but which can do the job even better. And since bacteria ubiquitously depend upon RNA polymerase to survive, blocking it with these new agents ought to be a sound strategy to deal with many of the world's most challenging infections, including the emerging multi-drug resistant forms of TB.