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. 2015 Mar 3;43(7):3841–3856. doi: 10.1093/nar/gkv172

Figure 8.

Figure 8.

Structural and sequence similarity between Hop2–Mnd1, Swi5-Sfr1 and Mei5–Sae3. (A) Comparison between Hop2–Mnd1 and Swi5–Sfr1C. Structural superposition reveals close structural similarity, but with different directions of the kinks. The protruding β-sheet of Swi5-Sfr1C was shown to be flexible in solution and dispensable for stimulation of Rad51 (54). (B) Comparison between Swi5–Sfr1 and Mei5–Sae3. Schematic drawings of the four proteins. The colored boxes and arrows indicate the homologous regions, whose sequences are aligned below. These regions exhibit sequence identity of 31% between Sae3 and Swi5 and 21% between Mei5 and Sfr1. Predicted (for Sae3 and Mei5) or structure-based (for Swi5 and Sfr1) secondary structure elements are shown above and below the alignment, respectively.