Literature DB >> 28471359

Crystal structure of the RNA 2',3'-cyclic phosphodiesterase from Deinococcus radiodurans.

Wanchun Han1, Jiahui Cheng1, Congli Zhou1, Yuejin Hua1, Ye Zhao1.   

Abstract

2',3'-Cyclic phosphodiesterase (CPDase) homologues have been found in all domains of life and are involved in diverse RNA and nucleotide metabolisms. The CPDase from Deinococcus radiodurans was crystallized and the crystals diffracted to 1.6 Å resolution, which is the highest resolution currently known for a CPDase structure. Structural comparisons revealed that the enzyme is in an open conformation in the absence of substrate. Nevertheless, the active site is well formed, and the representative motifs interact with sulfate ion, which suggests a conserved catalytic mechanism.

Entities:  

Keywords:  CPDase; Deinococcus radiodurans; RNA 2′,3′-cyclic phosphodiesterase; RNA repair

Mesh：

Substances：

Year:  2017        PMID： 28471359      PMCID： PMC5417317          DOI： 10.1107/S2053230X17004964

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN： 2053-230X            Impact factor:   1.056


  18 in total

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Authors:  K S Makarova; L Aravind; Y I Wolf; R L Tatusov; K W Minton; E V Koonin; M J Daly
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Authors:  Yongqing Liu; Jizhong Zhou; Marina V Omelchenko; Alex S Beliaev; Amudhan Venkateswaran; Julia Stair; Liyou Wu; Dorothea K Thompson; Dong Xu; Igor B Rogozin; Elena K Gaidamakova; Min Zhai; Kira S Makarova; Eugene V Koonin; Michael J Daly
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  1 in total

1.  Deinococcus radiodurans HD-Pnk, a Nucleic Acid End-Healing Enzyme, Abets Resistance to Killing by Ionizing Radiation and Mitomycin C.

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  1 in total

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