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. 2023 Jan 19;19(6):695–702. doi: 10.1038/s41589-022-01232-y

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© The Author(s) 2023

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. 2 — a, Superposition of the F₄₂₀H₂-oxidase domain in Fsr (MjFsr in dark green, MtFsr in light green) with FrhB from M. barkeri (black, PDB 6QGR) and FrhB from M. marburgensis (white, PDB 4OMF). The extended loops 171–189 in MjFsr and MtFsr are highlighted, as well as the lid, which is static in the Frh structures, but more flexible in Fsr (Extended Data Fig. 4b,c). b, Representation of MtFsr F₄₂₀H₂-oxidase domain (green surface) and its N-terminal ferredoxin domain (blue cartoon residues 1–70). The N terminus of Fsr and C terminus from the F₄₂₀H₂-oxidase domain are highlighted by blue and red spheres, respectively. The inserted ferredoxin domain, provided by the opposing monomer (Fsr′), is shown in white cartoon representation. c, Arrangement of FrhB (green surface) with FrhG (cartoon) from M. marburgensis (PDB 4OMF). The N-terminal part (45–205) of FrhG is colored in white and its C-terminal part (206–275), structurally equivalent to the N-terminal ferredoxin domain of Fsr, is colored in blue. The cyan ball highlights the connection between both FrhG parts.