Crystal structure of the site-specific recombinase, XerD.
The structure of the site-specific recombinase, XerD, that functions in circular chromosome separation, has been solved at 2.5 A 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.
Subramanya
H S
HS
Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.
Arciszewska
L K
LK
Baker
R A
RA
Bird
L E
LE
Sherratt
D J
DJ
Wigley
D B
DB
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D004254:DNA Nucleotidyltransferases / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D019426:Integrases; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D045522:Recombinases; D011995:Recombination, Genetic; D017386:Sequence Homology, Amino Acid; D013499:Surface Properties
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D045522:Recombinases; D004254:DNA Nucleotidyltransferases; D019426:Integrases; C115006:integron integrase IntI1