The protease state of the heat-shock protein DegP fromEscherichia coli

Abstract

Acta Cryst. (2007). A63, s120 nicks. Members of this ubiquitous family of structurespecific endonucleases function as dimers and require divalent cations for cleavage. We have solved the crystal structures of cruciform cutting enzyme 1 (CCE1) from Candida glabrata and Holliday junction cutting enzyme (Hjc) from the hyperthermophile archaeon Archaeoglobus fulgidus [1] at 3 and 1.7Å resolution, respectively. They represent two structurally distinct resolvase families with the same biological function, but exhibiting clearly different substrate specificities. Co-crystallization of these proteins with selected DNA substrates is under way.