Abstract
MCR (mobile colistin resistance) enzymes catalyse phosphoethanolamine (PEA) addition to bacterial lipid A, threatening the "last-resort" antibiotic colistin. Molecular dynamics and density functional theory simulations indicate that monozinc MCR supports PEA transfer to the Thr285 acceptor, positioning MCR as a mono- rather than multinuclear member of the alkaline phosphatase superfamily.
MeSH terms
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Alkaline Phosphatase / chemistry*
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Anti-Bacterial Agents / chemistry*
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Bacterial Proteins / chemistry*
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Colistin / chemistry*
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Drug Resistance, Bacterial*
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Ethanolamines / chemistry
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Lipid A / chemistry
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Molecular Dynamics Simulation
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Zinc / chemistry*
Substances
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Anti-Bacterial Agents
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Bacterial Proteins
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Ethanolamines
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Lipid A
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phosphorylethanolamine
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Alkaline Phosphatase
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Zinc
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Colistin