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Figure 1.
The binding site of oxazolidinones. (A) Secondary structure
of the peptidyltransferase ring of the 23S rRNA from D.
radiodurans with the mutation sites in bacteria (blue) and
archaea (purple) that confer resistance to oxazolidinones
indicated with E. coli numbering. Nucleotides that directly
interact with linezolid are shaded light blue, and the mutations
sites associated with resistance for chloramphenicol (cam) (45,
46), anisomycin (aniso) (47, 48), and pleuromutilins (pleuro)
(49) are shown. (B) Interface view of the D. radiodurans 50S
subunit with the binding position of linezolid (red) and
landmark proteins L1 and L11 as indicated. (C) Chemical
structure of linezolid, highlighting the three aromatic rings
(A–C) and the acetamidomethyl tail. (D) View of linezolid
(pink) within the binding pocket formed by eight universally
conserved nucleotides (blue) of the 23S rRNA. The arrow
indicates tunnel direction.
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