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. Author manuscript; available in PMC: 2011 Mar 2.
Published in final edited form as: DNA Repair (Amst). 2010 Jan 22;9(3):202–209. doi: 10.1016/j.dnarep.2009.12.009

Figure 2.

Figure 2

Amino acid motifs of E. coli PriA. PriA is divided into two major domains, a DNA-binding domain and a DNA helicase domain. The DNA helicase domain consists of an ATP-binding domain composed of a Walker A box, Walker B box, and SAT motif, and a cysteine-rich region that contains two Zn-finger motifs. Amino acid substitutions in the Walker A box, K230R, yielding a helicase-dead mutant protein, and in the metal binding domain, C479Y, representing the priA300 and priA301 mutations, are shown.