IUCr journals

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)

[Catalytic core] 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.

S. Réty, L. Rezábková, B. Dubanchet, J. Silhán, P. Legrand and A. Lewit-Bentley