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. Author manuscript; available in PMC: 2011 Jul 1.
Published in final edited form as: Arch Biochem Biophys. 2010 Sep 18;505(1):13–21. doi: 10.1016/j.abb.2010.09.012

Figure 6.

Figure 6

(A) Reaction catalyzed by the fosfomycin thiol transferase FosA. (B) Reaction catalyzed by the homologous FosX metalloenzyme that hydrates the antibiotic. (C) Structure of the fosfomycin inactivating enzyme FosA. (D) Close-up view of the active site of FosA. (E) Structure of the fosfomycin hydrolase FosX. (F) Close-up view of the active site of FosX revealing a glutamate residue (Glu44) that is proximal to the substrate and that is essential for catalysis. This residue is absent in FosA.