5h7e
From Proteopedia
Crystal Structure of native drCPDase
Structural highlights
FunctionO32509_DEIRD Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.[HAMAP-Rule:MF_01940] Publication Abstract from PubMed2',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 A 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. Crystal structure of the RNA 2',3'-cyclic phosphodiesterase from Deinococcus radiodurans.,Han W, Cheng J, Zhou C, Hua Y, Zhao Y Acta Crystallogr F Struct Biol Commun. 2017 May 1;73(Pt 5):276-280. doi:, 10.1107/S2053230X17004964. Epub 2017 Apr 26. PMID:28471359[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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