Structural highlights
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
