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. 2004 Jan 2;32(1):169–178. doi: 10.1093/nar/gkg925

Figure 1.

Figure 1

Sequence alignment of P.furiosus (Pf) and human (Hs) Rad51, Rad51B, Rad51C, murine (Mm) Rad51D, and human Xrcc2 and Xrcc3. Secondary structure for PfRad51 is shown schematically above the amino acid sequences, with cylinders for α-helices and arrows for β-strands, colored from blue to red, from the N- to the C-terminus, respectively. The helix preceding strand six, shown with a dashed line, is predicted in the Rad51 paralogs using PSI-PRED (46), but is absent in the PfRad51 crystal structure. Thin, horizontal colored lines indicate approximate regions of the N-terminal domain, the linker region, and the C-terminal domain by the colors blue, red and turquoise, respectively. The Walker A and Walker B ATP binding motifs are indicated by rectangles.