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. 2017 Jul 21;45(15):9019–9029. doi: 10.1093/nar/gkx620

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© The Author(s) 2017. 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 8. — Locations of conserved carboxylate residues in SPOUT methyltransferases. (A) Crystal structure of Saccharomyces cerevisiae Trm10 (PDB:4JWJ) (25) showing the positions of D210, D100 and E111. The S-adenosyl homocysteine is shown in green. (B) Crystal structure of Haemophilus influenzae TrmD (PDB: 4YVI) (40) showing the active site composed of residues from two subunits. The SAM analog (sinefungin in green) is bound to subunit A (opaque) and the catalytic residue D169* of subunit B (transparent) is shown in red.