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. 2015 Nov 24;44(1):342–353. doi: 10.1093/nar/gkv1306

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — CacKam possesses a conserved SAM-binding pocket. Comparison of residues forming the cosubstrate binding pocket in crystal structures of (A) CacKam-SAH, (B) KamB-SAH and (C) NpmA-SAM complexes. (D) View of the conserved and functionally essential water-mediated interactions in the SAM-binding pocket, shown for the CacKam-W203A complex with SAM. (E) WebLogo (41) plot of amino acid conservation in the SAM-binding pocket from ClustalW (42) alignment of unique 16S rRNA (m¹A1408) methyltransferase sequences. The CacKam residue type and number is shown under the plot.