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. 2023 Dec 7;31(1):150–158. doi: 10.1038/s41594-023-01124-2

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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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Extended Data Fig. 4 — (a) Sequence alignment of Azotobacter vinelandii Mo and V nitrogenase K-subunit (NifK and VnfK) to Rhodobacter capsulatus Fe nitrogenase K-subunit (AnfK). Identical sites are shown in green and similar sites (BLOSUM62 matrix⁶⁸ threshold of 2) that occur in 2 of 3 sequences are highlighted in yellow. (b) Structural alignment of the catalytic components of the Mo (PDB: 7UTA, resting-state catalytic component), V (PDB: 5N6Y, resting-state catalytic component), and Fe (PDB: 8OIE, AlF3-trapped complex) nitrogenases aligned in (a) and including the G-subunit for V and Fe nitrogenase. Inset at bottom shows a zoomed view of the αIII domain, with arrows depicting the origin in the sequence alignment. (c) Sequence alignment of Azotobacter vinelandii Mo and V nitrogenase D-subunit (NifD and VnfD) to Rhodobacter capsulatus Fe nitrogenase D-subunit (AnfD). Identical sites are shown in green and similar sites (BLOSUM62 matrix, threshold of 2) that occur in 2 of 3 sequences are highlighted in yellow. (d) Close-up view into the interface between individual DK-halves of the catalytic component. Arrow points towards C-terminus of D-subunit, which is extended in Fe nitrogenase. (e) Structural alignment of putty-styled cartoon Mo, V, and Fe nitrogenases (same models as in (b)). Putty size is scaled by B-factor. Mo (PDB: 7UTA, resting-state catalytic component) and Fe (PDB: 8OIE, AlF₃-trapped complex) nitrogenase structures are measured by cryo-EM, whereas V (PDB: 5N6Y, resting-state catalytic component) nitrogenase structure derives from X-ray crystallography.