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. 2019 Mar 17;16(6):798–808. doi: 10.1080/15476286.2019.1589360

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© 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 5. — Comparison of RlmJ:BA4(b) with RNA-bound m⁶A RNA and DNA MTases. (A) Comparison of the position of the substrate base of BA4(b) (blue) from RlmJ:BA4 and the corresponding base (A17) in the human homologue METTL16 co-crystallised with an RNA substrate (PDB: 6DU4) (orange). SAH (yellow) from RlmJ:SAH, aligned with RlmJ:BA4, is shown for comparison. The methylated bases and all cofactors are shown in stick representation. (B) As for A, but compared to the corresponding base (A606) from the DNA co-crystallised with m⁶A DNA MTase M.TaqI (PDB: 1G38) bound to the cofactor analogue 5′-[2-(amino)ethylthio]-5′-deoxyadenosine (AETA) (orange). (C) As for A, but compared to the corresponding base (A608) from the DNA co-crystallised with m⁶A DNA MTase T4Dam (PDB: 1YFL) bound to the cofactor analogue sinefungin (orange).