Structural highlights
Function
Q9RSC1_DEIRA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radiodurans.,Goncalves AM, Fioravanti E, Stelter M, McSweeney S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt, 11):1083-7. Epub 2009 Oct 13. PMID:19923723[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Goncalves AM, Fioravanti E, Stelter M, McSweeney S. Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radiodurans. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt, 11):1083-7. Epub 2009 Oct 13. PMID:19923723 doi:10.1107/S1744309109037191
