Extended Data Fig. 3: Comparison of the revisited AvNifEN and holo-GmNifEN structures.
From: Dynamics driving the precursor in NifEN scaffold during nitrogenase FeMo-cofactor assembly
a, Ribbon cartoon representation of the two structures (AvNifEN & holo-GmNifEN; left & right, respectively) in the same orientation as in Extended Data Fig. 2d. For clarity, only a single NifEN heterodimer is shown. The NifE subunit is depicted in solid colors, while the NifN subunit is shown with transparency. The three αβ-domains that constitute the NifE subunits are colored blue, red, and yellow (domains 1–3, respectively), while the connecting regions are shown in gray. The N-terminal regions defined in AvNifEN is highlighted in green. Cofactors are depicted in ball-and-stick representation. b, Close-up of the third αβ-domain of NifE, which exhibits all significant structural differences among the two structures (root mean square deviation: 3.1 Å overall, 1.5, 2.4 and 3.7 Å for NifE αβ-domains 1-3, respectively; Extended Data Fig. 2d). Disordered regions absent in the structures are indicated with the number of missing residues.
