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. 2021 Nov 20;2(1):36–52. doi: 10.1021/acsbiomedchemau.1c00044

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© 2021 The Authors. Published by American Chemical Society

Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/).

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(a) Sequence alignment of TiHydG and EcThiH primary structures. Red and white boxes indicate conserved and similar amino acids in the two proteins. TiHydG secondary structure elements are depicted on top. (b) SAXS-generated envelope for (left) a HydG mutant lacking the C-terminal domain, HydG^Δ91 from Thermoanaerobacter tengcongensis (Tte), and (right) wild-type TteHydG.⁵¹ The TiHydG crystal structure²⁷ without (left, blue ribbon representation) and with (right, blue and green ribbon representation) the C-terminal domain and auxiliary cluster (see main text) were placed in the envelope. [FeS] clusters are represented as van der Waals spheres.