Researchers
have discovered a molecular structure that could aid the design of
broad-spectrum antibiotics targeting an enzyme essential to every known strain
of bacteria. They've mapped the structure of that enzyme, called MraY, as it is
bound to the natural antibacterial muraymycin. The results show the enzyme
changes it shape to reveal a hidden binding pocket, which muraymycin connects
to like a two-pronged plug inserting into a socket.
By
capturing the interactions between bacteria and their natural killers,
researchers think they can provide the inspiration for developing new and
improved drugs. For instance, five different naturally-occurring antibiotics
target MraY, an enzyme responsible for building up the cell wall to shield
bacteria from outside attack. However, without knowing the structures involved,
researchers have been unable to develop drugs with the same effects.
For
further details, see:
Ben C. Chung, Ellene H. Mashalidis, Tetsuya
Tanino, Mijung Kim, Akira Matsuda, Jiyong Hong, Satoshi Ichikawa, Seok-Yong
Lee. Structural insights into inhibition of lipid I production in
bacterial cell wall synthesis. Nature, 2016; DOI: 10.1038/nature17636
Posted by Dr. Tim Sandle