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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 1. — The conserved β-sheet core of the 16S rRNA (m¹A1408) methyltransferase family. Class I methyltransferases possess a structurally conserved, seven-stranded β-sheet (β1 to β7) with a central topological switch point (black dot) that creates the SAM-binding pocket. The conserved β-sheet core of the 16S rRNA (m¹A1408) methyltransferases is extended by a short N-terminal extension (β-N1 and β-N2, separated by the vertical dotted line). Structures shown are NpmA (cyan; PDB code 3MTE), KamB (orange; 3MQ2), Kmr (yellow; 4RWZ) and CacKam from C. acidiphilia (green cartoon; this study). The bound SAM (semi-transparent cyan sticks) is from the crystal structure of the NpmA–SAM complex (3MTE).