Extended Data Fig. 3: Structural details of NosDFY.
From: Molecular interplay of an assembly machinery for nitrous oxide reductase
a, NosD, coloured from blue at the N terminus to red at the C terminus (marked). Helices hI, hII and hIII interact with NosY. b, The ATPase domain NosF with the C-terminal R domain. c, The transmembrane domain NosY, with the second protomer coloured in white. d, In the NosF dimer, the R domains are crossed, providing additional stability. e, In the nucleotide-free state, the R domain was found in an ensemble of conformations that could be individually refined and revealed a high degree of structural flexibility. f, Superposition of NosD (green) with its closest structural relative, the CASH family protein DFA-IIIase (PDB 5ZKS, r.m.s.d. = 2.68 Å). g, NosF (light orange) and the related ABC domain MalK of the E. coli maltose importer (PDB 3RLF, r.m.s.d. = 2.05 Å). Note that although MalK contains an additional C-terminal domain, it shows no relevant similarity to the R domain. h, NosY (red) and the TMD of the Wzm/Wzt O-antigen transporter (PDB 6M96, r.m.s.d. = 6.0 Å).
