The structure of the site-specific recombinase, XerD, that functions i
n circular chromosome separation, has been solved at 2.5 Angstrom reso
lution and reveals that the protein comprises two domains, The C-termi
nal domain contains two conserved sequence moths that are located in s
imilar positions in the structures of XerD, lambda and HP1 integrases.
However, the extreme C-terminal regions of the three proteins, contai
ning the active site tyrosine, are very different, In XerD, the arrang
ement of active site residues supports a cis cleavage mechanism, Bioch
emical evidence for DNA bending is encompassed in a model that accommo
dates extensive biochemical and genetic data, and in which the DNA is
wrapped around an alpha-helix in a manner similar to that observed for
CAP complexed with DNA.