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. Author manuscript; available in PMC: 2016 Apr 7.
Published in final edited form as: Curr Opin Struct Biol. 2011 Dec 6;22(1):72–79. doi: 10.1016/j.sbi.2011.11.001

Figure 3.

Figure 3

Domain organization and structures of type II partition proteins. (a) Top, schematic diagram showing the domain arrangement of type II CBPs. Below is the structure of the pSK41 partition complex superstructure [33]. Shown to the side is one ParR dimer-of-dimer. (b) Domain organization of type II NTPases, which contain actin-like folds. Below is shown the recent structure of the pSK41 ParM protein and to the side is the EM reconstruction of the R1 ParM filament [35–36]. The pSK41 ParM subunit is shown in a similar orientation as the green R1 subunit in the filament to underscore the finding that the regions that make interactions important for filamentation are not conserved between the two structures. This explains why pSK41 ParM forms filaments that are distinct from R1 ParM.