Fig. 2 | Nature Communications

Fig. 2

From: The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile

Fig. 2

Structure of the EtfAB/Bcd complex. a The heterododecameric (EtfAB/Bcd)4 complex. Tetrameric Bcd (grey) forms the core and the four EtfAB units are peripherally associated (domain I in brown, domain II in red and domain III in green). b EtfAB/Bcd of C. difficile in the D state. The catalytic reaction involves domain I (brown) of EtfA and domain III of EtfB (green) forming the EtfAB base and a Bcd dimer (Bcd1 in grey and Bcd2 in light blue). Each of the three subunits Bcd, EtfA and EtfB non-covalently binds one FAD (isoalloxazine in yellow). c The EtfAB/Bcd complex in the B-like state. Domain II is rotated nearly 80° such that α-FAD and β-FAD are nearly in a distance suitable for ET. α-FAD embedded into the weakly associated domain II serves as a one-electron shuttle between the electron-donating β-FADH− and the electron-accepting δ-FAD

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