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.
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作者:Gonçalves A M D, Fioravanti E, Stelter M, McSweeney S
| 期刊: | Acta Crystallographica Section F-Structural Biology and Crystallization Communications | 影响因子: | 1.100 |
| 时间: | 2009 | 起止号: | 2009 Nov 1; 65(Pt 11):1083-7 |
| doi: | 10.1107/S1744309109037191 | ||
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