Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radiodurans.
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.
Gonçalves
A M D
AM
Macromolecular Crystallography Group, European Synchrotron Radiation Facility, Grenoble, France.
Fioravanti
E
E
Stelter
M
M
McSweeney
S
S
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D034301:Deinococcus / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011755:Pyrophosphatases / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D000096964:Nudix Hydrolases
D001426:Bacterial Proteins; D011755:Pyrophosphatases; D000096964:Nudix Hydrolases