Structural studies of the catalytic core of the primate foamy virus (PFV-1) integrase

Acta Cryst. (2010). F66, 881-886 (doi.org/10.1107/S1744309110022852)

Structure of the dimer of PFV-1 integrase catalytic core with manganese (orange sphere). The residues of the catalytic triad are shown as ball-and-sticks. Water molecules involved in manganese ion coordination are shown in red.

Integrases are key enzymes for the integration of retroviral genomes into host cell DNA. Cations, either Mg²⁺ or Mn²⁺, bound to the catalytic core which carries the catalytic triad D-D35E, are essential for all activities of the protein. We determined structures of the catalytic core of the human foamy virus with and without Mg²⁺ and Mn²⁺, which show the effect of cations on the conformation of the active site and thus give hints into the catalytic mechanism.