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. 2020 Mar 18;11:1426. doi: 10.1038/s41467-020-15214-y

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© The Author(s) 2020

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 Structure of the AdhE monomer in the presence of NAD⁺ and Fe²⁺. The AlDH and ADH domains are identified. In each domain, the electron density corresponding to the NAD⁺ and Fe²⁺ is displayed in green mesh, as it is visible in the cryoEM map. In the lower part of the panel, larger views of the cofactor-binding sites are provided. b Structure of the AdhE dimer in its extended conformation. The AdhE_n dimer is made of the α (in light blue) and β (in blue) protomers. Each protomer is composed of ADH and AlDH domains. The AdhE_n dimer is in interaction with the ADH_n − 1 and ADH_n + 1. The AdhE_α and AdhE_β are related by C2 symmetry. c Structural model of the AdhE filament in its extended conformation. This model was obtained by docking the structure of the AdhE dimer shown in b, in the cryoEM map obtained by HR and by duplicating this dimer along the filament axis using its helical symmetry. d Structure of the AdhE monomer in the presence of NADH and Fe²⁺. The AlDH and ADH domains are identified. In the ADH domain, the electron density corresponding to the NADH and Fe²⁺ is displayed in green mesh, as it is visible in the cryoEM map. No density corresponding to the NADH is visible in the AlDH domain active site. In the lower part of the panel, larger views of the ADH cofactor-binding site are provided. e Structure of the AdhE dimer in its compact conformation. The AdhE_n dimer is made of the α (in light blue) and β (in blue) protomers. Each protomer is composed of ADH and AlDH domains. The AdhE_n dimer is in interaction with the ADH_n − 1 and ADH_n + 1. The AdhE_α and AdhE_β are related by C2 symmetry. f Structural model of the AdhE filament in its compact conformation. This model was obtained by docking the structure of AdhE dimer shown in d, in the cryoEM map obtained by HR and by duplicating this dimer along the filament axis using its helical symmetry.