Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage.

ABSTRACT: Overcoming lysogenization defect (OLD) proteins constitute a family of uncharacterized nucleases present in bacteria, archaea, and some viruses. These enzymes contain an N-terminal ATPase domain and a C-terminal Toprim domain common amongst replication, recombination, and repair proteins. The in vivo activities of OLD proteins remain poorly understood and no definitive structural information exists. Here we identify and define two classes of OLD proteins based on differences in gene neighborhood and amino acid sequence conservation and present the crystal structures of the catalytic C-terminal regions from the Burkholderia pseudomallei and Xanthamonas campestris p.v. campestris Class 2 OLD proteins at 2.24 Å and 1.86 Å resolution respectively. The structures reveal a two-domain architectur

SUBMITTER: Schiltz CJ 

PROVIDER: S-EPMC6755086 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature