Structural Recognition of Spectinomycin by Resistance Enzyme ANT(9) from Enterococcus faecalis
Sandesh Kanchugal P, M. Selmer
Abstract
loop, which would clash with the larger streptomycin substrate. In the active site, we observed two magnesium ions, one of them in a previously unobserved position that may activate the 9-hydroxyl for deprotonation by the catalytic base Glu-86. The observed binding mode for spectinomycin suggests that spectinamides and aminomethyl spectinomycins, recent spectinomycin analogues with expansions in position 4 of the C ring, are also subjected to modification by ANT(9) and ANT(3")(9) enzymes.
Topics & Concepts
SpectinomycinEnterococcus faecalisBiochemistryBinding siteChemistryBiologyStereochemistryStreptomycinAntibioticsEscherichia coliGeneBiochemical and Molecular ResearchEnzyme Structure and FunctionRNA and protein synthesis mechanisms