Abstract
MCR-2 confers resistance to colistin, a `last-line' antibiotic against extensively resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanolamine transferase that is closely related to MCR-1. To understand the diversity in the MCR family, the 1.12 Å resolution crystal structure of the catalytic domain of MCR-2 was determined. Variable amino acids are located distant from both the di-zinc active site and the membrane-proximal face. The exceptionally high resolution will provide an accurate starting model for further mechanistic studies.
Keywords:
MCR-1; MCR-2; antibiotic resistance; colistin; polymixin.
MeSH terms
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Amino Acid Sequence
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Catalytic Domain
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Cloning, Molecular
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Colistin / chemistry*
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Colistin / metabolism
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Crystallography, X-Ray
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Drug Resistance, Bacterial
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Escherichia coli / chemistry*
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism
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Gene Expression
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Genetic Vectors / chemistry
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Genetic Vectors / metabolism
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Models, Molecular
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Plasmids / chemistry*
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Plasmids / metabolism
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Protein Binding
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Protein Conformation, alpha-Helical
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Protein Conformation, beta-Strand
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Protein Interaction Domains and Motifs
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Protein Isoforms / chemistry
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Protein Isoforms / genetics
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Protein Isoforms / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Alignment
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Structural Homology, Protein
Substances
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Escherichia coli Proteins
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MCR-1 protein, E coli
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Protein Isoforms
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Recombinant Proteins
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Colistin