Fig. 2: Unique features of RAD51–X3C.
From: Structural insight into how RAD51 paralog exchange regulates RAD51 filament formation
a, Cartoon representations of the indicated complexes, with AMP-PNP (nonhydrolyzable ATP analog) and DNA shown as spheres. RAD51C from the BCDX2 complex and RAD51.1 from the presynaptic RAD51 filament were superimposed onto RAD51.A2 from the RAD51–X3C structure. XRCC3 from the A. pompejana crystal structure was superimposed onto XRCC3 from RAD51–X3C. b, Subcomplexes from the RAD51–X3C structure (RAD51C–XRCC3, RAD51.A2–XRCC3 and RAD51.A1–RAD51.A2) are shown side by side to compare subunit organization. Right: the RAD51 presynaptic filament is shown for reference. c, Structural analysis of the regions corresponding to the canonical RAD51 polymerization motif in the RAD51–X3C complex. d, Structure-based sequence alignment of the RAD51 polymerization motif. e, Structure-based sequence alignment of the RAD51 polymerization motif-binding pocket. Residues corresponding to the canonical RAD51 motif and binding pocket are boxed in red; divergent positions among RAD51 paralogs are indicated by stars above the alignment.
