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  • The EMBO Journal (1997) 16, 5178 - 5187
  • doi:10.1093/emboj/16.17.5178

Crystal structure of the site-specific recombinase, XerD

Hosahalli S. Subramanya1, Lidia K. Arciszewska2, Rachel A. Baker2, Louise E. Bird1, David J. Sherratt1 and Dale B. Wigley1

  1. Laboratory of Molecular Biophysics, University of Oxford, Oxford OX1 3QU, UK
  2. Microbiology Unit, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK

Correspondence to:

David J. Sherratt, E-mail: Sherratt@bioch.ox.ac.uk

Received 21 May 1997; Revised 26 June 1997

The structure of the site-specific recombinase, XerD, that functions in circular chromosome separation, has been solved at 2.5 Å resolution and reveals that the protein comprises two domains. The C-terminal domain contains two conserved sequence motifs that are located in similar positions in the structures of XerD, lambda and HP1 integrases. However, the extreme C-terminal regions of the three proteins, containing the active site tyrosine, are very different. In XerD, the arrangement of active site residues supports a cis cleavage mechanism. Biochemical evidence for DNA bending is encompassed in a model that accommodates 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.

  • Keywords:

    • DNA binding,
    • recombination mechanism,
    • site-specific recombinase,
    • XerD structure