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. 2017 Nov 22;7:16027. doi: 10.1038/s41598-017-16266-9

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© The Author(s) 2017

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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Crystal structure of the tropical AKDr. (a) Overall structure of AKDr. The CORE (residues 1–38, 69–136, and 143–194), AMP_bind (residues 39–68) and LID (residues 137–142) domains are shown in orange, blue, and red, respectively. The co-crystallized Ap₅A molecule is shown in black. (b,c) Hydrophobic contacts of Ile28 (b) and Ile118/Ile173 (c) in the CORE domain of the AKDr structure. The three Ile residues are substituted to Val residues in AKNc. The 2mF_obs−DF_calc map is contoured at 1.0 σ. (d,e) Close-up views of Ala48 (d) and Lys188 (e) in the crystal structure of AKDr. Ala48 and Lys188 are conserved among the three tropical AKs including AKDr, but not in AKNc. The side chains of Ala48 and Lys188 are exposed to the solvent, and do not interact closely with residues that are located distantly in the amino acid sequence.