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. 2020 Feb 13;53:6. doi: 10.1186/s40659-020-00274-7

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 1 — Topology, functional motifs, and domains of M. tuberculosis CtpB. a The predicted topology of CtpB shows eight TM helices (1 to 8), locating the N- and C-terminal ends within the cytoplasmic portion. The cytoplasmic domains are represented by stitched lines and the functional motifs of P_1B-type ATPase are shown. The amino acids responsible for cation coordination within TM segments 6, 7 and 8 are highlighted in bold. b The TM helices were predicted using TOPCONS. The multiple alignment of the N-terminal end, TM6, TM7, and TM8 of CtpB and other bacterial characterized Cu⁺-ATPases (CopA from Archaeoglobus fulgidus (WP_010877980.1) and Legionella pneumophila (YP_095057.1)) was constructed using Clustal Omega. Some of the amino acids involved in the coordination of Cu⁺ are located within TM6, 7 and 8. The residues are classified as nonpolar (black), polar (green), acid (blue), and basic (red)