Erythromycin resistance methyltransferases (Erms) cause resistance to macrolide antibiotics by methylation of A2058 of 23S ribosomal RNA. Found in the exit tunnel of a bacterial ribosome, this position sits in the binding site for macrolide antibiotics, which interfere with nascent polypeptide extrusion to inhibit bacterial protein synthesis. Though the function and site of methylation is known for Erm enzymes, the details of enzyme-substrate interaction are still being uncovered. Structurally, Erm proteins are made of a Rossmann fold N-terminal domain connected to a C-terminal domain through a 10 amino acid linker. Using site-saturation mutagenesis, we investigated the significance of the Erm linker region in enzyme function for ErmE and ErmC.

Structural determinants of substrate selection in erythromycin resistance methyltransferases

2019 Spring National Meeting

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