Work

Structure of an N-terminally truncated Nudix hydrolase DR2204 fromDeinococcus radiodurans

Year: 2009

Type: article

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.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309109037191

Authors: A. M. D. Gonçalves, E. Fioravanti, M. Stelter, S. McSweeney

Institution: European Synchrotron Radiation Facility

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze

OpenAlex ID: W1991228091

FWCI: 0.161

Cites: 38

Cited by: 3

Related to: 10