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. 2021 Jun 7;4:687. doi: 10.1038/s42003-021-02147-5

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© The Author(s) 2021

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 — The observed [2Fe-2S] cluster of AtAcnX in the apo-form (a) and in complex with C3LHyp (b) of the wild-type enzyme, and in the apo-form of the S449C/C510V mutant (c). The observed [3Fe-4S] cluster of TkAcnX in the apo-form (d) and in complex with MVA5P (e). 2mF_o–DF_c electron density maps for the [Fe-S] cluster, contoured at 1.5 σ, are shown as a gray mesh. Anomalous difference Fourier maps, contoured at the 5.0 σ (a), 3.0 σ (b), 4.0 σ (c), 3.0 σ (d), and 9.0 σ levels (e), indicate peaks for Fe atoms, and are shown as a blue mesh. Superposition of [Fe-S] clusters of AtAcnX (f), TkAcnX (g), mAcn (h; 6ACN), and IPMI (i; 4KP2) within its active sites, ligated to protein cysteines by Fe-S bonds. Amino-acid residues located at equivalent (or close) positions are indicated in the same color and correspond to Fig. 2. The hypothetically activated [4Fe-4S] cluster of TkAcnX, the Fe2 atom, and a water molecule (gray) appeared to be coordinated to the [3Fe-4S] cluster.