2W4E

Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radiodurans

2W4E の概要

• エントリーDOI: 10.2210/pdb2w4e/pdb
• 分子名称: MUTT/NUDIX FAMILY PROTEIN (2 entities in total)
• 機能のキーワード: adp-ribose pyrophosphatase, hydrolase
• 由来する生物種: DEINOCOCCUS RADIODURANS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31213.73

構造登録者

Goncalves, A.M.D.,Fioravanti, E.,Stelter, M.,McSweeney, S. (登録日: 2008-11-25, 公開日: 2009-12-01, 最終更新日: 2024-05-08)

主引用文献

Goncalves, A.M.D.,Fioravanti, E.,Stelter, M.,Mcsweeney, S.
Structure of an N-Terminally Truncated Nudix Hydrolase Dr2204 from Deinococcus Radiodurans.
Acta Crystallogr.,Sect.F, 65:1083-, 2009

PubMed 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.

PubMed: 19923723
DOI: 10.1107/S1744309109037191

実験手法

X-RAY DIFFRACTION (2 Å)