Bacteria use diverse mechanisms to overcome antibiotics, including their destruction or chemical modification. Rifamycins, which are semi-synthetic antibiotics, adopt a characteristic basket-like structure that is essential for binding to the RNA exit tunnel of the target β-subunit of bacterial RNA polymerase to inhibit RNA synthesis. In this study, Wright and colleagues report the structure and function of a rifamycin monooxygenase (Rox) from Streptomyces venezuelae that inactivates a broad range of rifamycins. They determined the crystal structure of the Rox and identified a new molecular mechanism of resistance: monooxygenation of the C2 naphthyl ring, which results in ring opening and subsequent linearization of the antibiotic. The altered conformation prevents the antibiotic from binding to its target.
References
Koteva, K., Cox, G., Kelso, J. K. et al. Rox, a rifamycin resistance enzyme with an unprecedented mechanism of action. Cell Chem. Biol. https://doi.org/10.1016/j.chembiol.2018.01.009 (2018)
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Du Toit, A. Bacterial enzymes 'straighten out' antibiotics. Nat Rev Microbiol 16, 122 (2018). https://doi.org/10.1038/nrmicro.2018.19
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DOI: https://doi.org/10.1038/nrmicro.2018.19
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