Extended Data Fig. 6: More splayed conformation of monomeric MgtA structure relative to the dimer with major changes in TM1-4, N and A domains.
From: P-type ATPase magnesium transporter MgtA acts as a dimer
a, Dimeric structure with two subunits in two different gray tones and Mg2+ ions as green spheres. b, Monomeric structure colored as in Fig. 1. c-d, To visualize structural changes the colored monomer and a single dimer subunit in gray were superimposed (c) and RMSD was calculated (d). The monomer structure is shown colored by RMSD indicating the largest differences when comparing the two structures by high RMSD values in red. e-f, Structural differences between the dimer (gray) and monomer (purple) for TM1-2 (e) and TM3-4 (f). The monomer colored according to RMSD is on the right with densities in mesh indicating the fit. g, Monomer density features and fitted model of TM5 and TM7 near ion-binding site A in the middle of the membrane which is similar to the dimer structures. h-j, Differences in position in the overall conformation between the soluble domains of the dimer (gray) and monomer (colored).
