Emergence of plasmid-mediated colistin resistance mechanism MCR-1 in animals and human beings in China: a microbiological and molecular biological study.
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mcr-1 is the first plasmid-mediated, horizontally transferable colistin-resistance determinant; it confers polymyxin resistance and was found in E. coli from animals and humans.
"Emergence of plasmid-mediated colistin resistance mechanism MCR-1 in animals and human beings in China"
Structure of the catalytic domain of the colistin resistance enzyme MCR-1.
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MCR-1 is a phosphoethanolamine transferase that catalyses addition of phosphoethanolamine to lipid A; the periplasmic catalytic domain has an alkaline-phosphatase-like fold with active-site zinc, and Thr285 is the phosphoethanolamine-modified catalytic residue.
"MCR-1 is a phosphoethanolamine transferase that catalyzes the addition of phosphoethanolamine to lipid A"
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Resistance arises from modification of the 1' and 4' phosphate groups of lipid A, neutralising the negative charge and reducing binding of cationic colistin.
"modification of the 1' and 4' phosphate groups of lipid A to neutralize the negative charge and reduce binding of the positively charged colistin"
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A zinc is present at a conserved active-site position, consistent with a metal-dependent enzyme.
"a zinc is present at a conserved site in addition to three zincs more peripherally located in the active site"
Substrate analog interaction with MCR-1 offers insight into the rising threat of the plasmid-mediated transferable colistin resistance.
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MCR-1 catalyses transfer of phosphoethanolamine to lipid A, the reaction underlying colistin resistance.
"can catalyze the transfer of phosphoethanolamine (PEA) to lipid A, resulting in"
Gene Ontology annotation through association of InterPro records with GO terms
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
Blinded OpenScientist function-assignment report (TreeGrafter audit)
Existing falcon function-hypothesis report