What is it about?
We identified a novel inhibitor of polymyxin resistant and determined the complex structure of MCR-1 catalytic domain with the inhibitor and another substrate analog, highlighting 2 possible substrate-binding pockets. Our work also illustrates the integrated catalytic and substrate-binding region right beside the positively charged region of N-terminal TM domain, suggesting the deep involvement of TM domain in the substrate binding.
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Why is it important?
MCR-1 is the newly reported plasmid-mediated phosphoethanolamine transferase conferring resistance to polymyxin, which is the last-line antibiotic used to treat multidrug resistant bacterial infections. Our drug candidate is the first specific inhibitor to inhibit the polymyxin resistance.
Perspectives
Our drug candidate could be good templates for further drug development and could also be effective inhibitor on polymyxin resistance by EptA or EptC.
lei yin
Wuhan University
Read the Original
This page is a summary of: Substrate analog interaction with MCR-1 offers insight into the rising threat of the plasmid-mediated transferable colistin resistance, The FASEB Journal, February 2018, Federation of American Societies For Experimental Biology (FASEB),
DOI: 10.1096/fj.201700705r.
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