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

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.

SUBMITTER: Han W

PROVIDER: S-EPMC5417317 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

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

Han Wanchun W Cheng Jiahui J Zhou Congli C Hua Yuejin Y Zhao Ye Y

Acta crystallographica. Section F, Structural biology communications 20170426 Pt 5

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 ...[more]

PMID: 28471359

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