Journal
SCIENTIFIC REPORTS
Volume 6, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep19524
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Funding
- Biotechnology and Biological Sciences Research Council (UK) [BB/H018433/1]
- BBSRC [BB/H018433/1] Funding Source: UKRI
- MRC [MC_U117533887] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H018433/1] Funding Source: researchfish
- Medical Research Council [MC_U117533887] Funding Source: researchfish
- The Francis Crick Institute [10029] Funding Source: researchfish
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Antibiotic resistance in clinically important bacteria can be mediated by proteins that physically associate with the drug target and act to protect it from the inhibitory effects of an antibiotic. We present here the first detailed structural characterization of such a target protection mechanism mediated through a protein-protein interaction, revealing the architecture of the complex formed between the FusB fusidic acid resistance protein and the drug target (EF-G) it acts to protect. Binding of FusB to EF-G induces conformational and dynamic changes in the latter, shedding light on the molecular mechanism of fusidic acid resistance.
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