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. 2016 Jun 20;44(13):6377–6390. doi: 10.1093/nar/gkw561

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© The Author(s) 2016. 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-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 3. — The SAM-binding site of _TkoTrm11 in complex with SAM. (A) Close-up view of the SAM molecule and its binding residues illustrated as stick models (magenta and cyan, respectively). Electron density map around the SAM molecule contoured at 2.0 σ. (B) Ligplot diagram (64) of interactions between _TkoTrm11 amino acid residues and the bound SAM molecule. (C) Methyl transfer activity of the alanine-substituted mutant proteins. The mutant name indicates the site of alanine substitution. The initial velocity of wild-type (WT) _TkoTrm11 is expressed as 100%. Error-bar indicates the SD (standard deviation) that was calculated between three independent experiments.