Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radiodurans

摘要

Nudix pyrophosphatases are a well represented protein family in the Deino­coccus radiodurans genome. These hydrolases, which are known to be enzymatically active towards nucleoside diphosphate derivatives, play a role in cleansing the cell pool of potentially deleterious damage products. Here, the structure of DR2204, the only ADP-ribose pyrophosphatase in the D. radio­durans genome that is known to be active towards flavin adenosine dinucleotide (FAD), is presented at 2.0 Å resolution.