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. 2017 Jul 21;7:6179. doi: 10.1038/s41598-017-05268-2

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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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Lcp has a globin fold and similarities to globin-coupled sensor proteins. Three-dimensional structure of Lcp_K30 (stereo image), coloured from blue at the N-terminus to red at the C-terminus (A). Helix designations follow the standard globin nomenclature. Note that Lcp_K30 contains an additional helix, L, in the globin domain. Domain structure of Lcp_K30 (B). A central domain with a globin fold (green) is capped by an N-terminal domain with three helices (N1-3, blue) and a C-terminal domain consisting of 6 helices (Z1-6, red). Secondary structures of sperm whale myoglobin (PDB-ID 1MBN) (C), the globin-coupled sensor protein of G. sulfurreducens (PDB-ID 2W31) (D) and the central domain of Lcp_K30 (E) highlight the conserved topology of the globin folding core, as well as substantial variations in helix arrangement and haem accessibility. The haem groups including their axial ligands are shown as sticks in (A,C,D,E).