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. 2019 Mar 21;10:1303. doi: 10.1038/s41467-019-09310-x

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — Comparison of JMJ13 and other histone demethylases. a A superposition of the JMJ13-NOG-H3K27me3 complex (in green) and UTX-NOG-H3K27me3 (in orange, PDB code: 3AVR) shows the similar overall structures and peptide-binding sites. b The structures of the C4HCHC dual zinc finger of JMJ13 (left panel, in green) and the C4 single zinc finger of UTX (right panel, in orange) showing different zinc coordination but similar folding topology. c The superposition of the JMJ13-NOG-H3K27me3 complex (in green) and the UTX-NOG-H3K27me3 (in orange) shows that the two proteins employ correspondent residues Asp236 of JMJ13 and Asp1089 of UTX to recognize H3R26 in the two complexes, respectively. In contrast, JMJ13 recognize H3S28 by a side chain hydrogen bond with Asp296, but UTX lacks this recognition. d The superposition of the JMJ13-NOG-H3K27me3 complex (in green) and UTX-NOG-H3K27me3 (in orange) shows that JMJ13 recognizes H3P30 by Phe179, while UTX recognizes H3P30 by Pro1144 at different positions. e A superposition of JMJ13-NOG-H3K27me3 complex (in green) and JMJ14-NOG-H3K4me3 complex (in magenta, PDB code: 5YKO) shows almost identical overall structures. f A detailed view of the comparison of the zinc finger domains of JMJ13 (in green) and JMJ14 (in magenta). The two zinc finger domains possess similar overall structures with the first zinc ions occupying the same position but the second zinc ions located at different positions. g The detailed structures of the zinc coordination of two zinc ions from JMJ13 (upper panel, in green) and the JMJ14 (lower panel, in magenta) show that the first zinc ions have the same coordination but the second ones have different coordination. h The schematic representation of the sequence motif and coordination of the zinc ions of the JMJ13 C4HCHC domain (upper panel) and JMJ14 C5HC2 domain (lower panel). The spacing residues are denoted as X