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. 2020 Sep 4;117(38):23548–23556. doi: 10.1073/pnas.2007391117

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Fig. 2. — Structure of human SDHA-SDHAF2 assembly intermediate. (A) The SDHA-SDHAF2 assembly intermediate in cartoon representation with the flavin-binding domain in white, the capping domain in gray, and SDHAF2 in cyan. The ligands are shown as sticks with the carbon atoms of the FAD in yellow and the carbon atoms of the oxaloacetate in black. (B) The hydrogen bond between SDHA^H99 and SDHAF2^G78. SDHA^H99 is the covalent ligand to FAD and this interaction is proposed to stabilize the orientation of this side chain during the flavinylation reaction. (C) Surface representation of SDHAF2 (cyan) superimposed with the E. coli homolog SdhE (wheat) from the FrdA-SdhE assembly intermediate (PDB ID 6B58) (22) illustrates the significantly larger interaction surface of SDHAF2 resulting from the extended N and C termini. The view is rotated 90° with respect to A. (D) Overlay of human SDHAF2 with E. coli SdhE (PDB ID 6B58) (22) highlights the extended N and C termini (red) of SDHAF2 and illustrates that these lack appreciable secondary structure.