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来自耐辐射球菌的N端截短的Nudix水解酶DR2204的结构

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

作者信息

Gonçalves A M D, Fioravanti E, Stelter M, McSweeney S

机构信息

Macromolecular Crystallography Group, European Synchrotron Radiation Facility, Grenoble, France.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt 11):1083-7. doi: 10.1107/S1744309109037191. Epub 2009 Oct 13.

DOI:10.1107/S1744309109037191
PMID:19923723
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2777031/
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.

摘要

Nudix焦磷酸酶是耐辐射球菌基因组中一个有充分代表性的蛋白质家族。这些水解酶对核苷二磷酸衍生物具有酶活性，在清除细胞中潜在有害的损伤产物方面发挥作用。本文展示了DR2204的结构，它是耐辐射球菌基因组中唯一已知对黄素腺嘌呤二核苷酸（FAD）有活性的ADP核糖焦磷酸酶，分辨率为2.0埃。

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