Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radiodurans
A M D Gonçalves1, E Fioravanti, M Stelter
1Macromolecular Crystallography Group, European Synchrotron Radiation Facility, Grenoble, France.
Abstract:
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 angstrom resolution.
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