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Clostridioides difficile  infections are an urgent medical problem. The newly discovered   C.    difficile   a denine  m ethyltransferase  A  (CamA) is specified by all  C. difficile  genomes sequenced to date (>300), but is rare among other bacteria. CamA is an orphan methyltransferase, unassociated with a restriction endonuclease. CamA-mediated methylation at CAAAA A  is required for normal sporulation, biofilm formation, and intestinal colonization by  C. difficile . We characterized CamA kinetic parameters, and determined its structure bound to DNA containing the recognition sequence. CamA contains an N-terminal domain for catalyzing methyl transfer, and a C-terminal DNA recognition domain. Major and minor groove DNA contacts in the recognition site involve base-specific hydrogen bonds, van der Waals contacts and the Watson-Crick pairing of a rearranged A:T base pair. These provide sufficient sequence discrimination to ensure high specificity. Finally, the surprisingly weak binding of the methyl donor  S -adenosyl- l -methionine (SAM) might provide avenues for inhibiting CamA activity using SAM analogs.

Clostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helix