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The 2.7 Å resolution crystal structure of the CcbJ methyltransferase from S. caelestis, which is part of the biosynthetic pathway of the lincosamide antibiotic celesticetin, is reported along with its complex with S-adenosyl-L-homocysteine at 2.9 Å resoution. Mutational and docking studies based on these structures are used to propose a plausible mechanism for its activity.
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