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d-alanine-d-lactate ligase from Enterococcus faecium BM4147 is directly responsible for the biosynthesis of alternate cell-wall precursors in bacteria, which are resistant to the glycopeptide antibiotic vancomycin. The crystal structure has been determined with data extending to 2.5-A resolution. This structure shows that the active site has unexpected interactions and is distinct from previous models for d-alanyl-d-lactate ligase mechanistic studies. It appears that the preference of the enzyme for lactate as a ligand over d-alanine could be mediated by electrostatic effects and/or a hydrogen-bonding network, which principally involve His-244. The structure of d-alanyl-d-lactate ligase provides a revised interpretation of the molecular events that lead to vancomycin resistance.

proceedings of the national academy of sciences of the united states of america

The molecular basis of vancomycin resistance in clinically relevant <i>Enterococci:</i> Crystal structure of <scp>d</scp> -alanyl- <scp>d</scp> -lactate ligase (VanA)

The molecular basis of vancomycin resistance in clinically relevant Enterococci: Crystal structure of d -alanyl- d -lactate ligase (VanA)