H
IPR009097

Cyclic phosphodiesterase

InterPro entry
Short nameCyclic_Pdiesterase
Overlapping entries
 

Description

This entry represents a β-barrel domain consisting of a duplication of a β/α/β/α/β motif, which is found in plant cyclic phosphodiesterases (CPDases)
[3]
, as well as catalytic domains from mammalian 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase)
[1]
, and bacterial and archaeal LigT-like 2',3'-cyclic phosphodiesterases (originally identified as 2'-5' RNA ligases)
[2]
. This β-barrel domain is similar in structure to the β-barrel found in prokaryotic DNA topoisomerases I and III.

The catalytic domain of CNPase from animals catalyses the hydrolysis of nucleoside 2',3'-cyclic monophosphates to nucleoside 2'-monophosphates
[5]
. The archaeobacterial LigT-like enzymes hydrolyze 2',3'-cyclic phosphate in (oligo)nucleotides and join the produced 2'-phosphate to a 5'-hydroxyl group of another (oligo)nucleotide to form atypical 2',5'-linkages. Such activity has not been reported for CNPase
[4]
.

References

1.Solution structure of the catalytic domain of RICH protein from goldfish. Kozlov G, Denisov AY, Pomerantseva E, Gravel M, Braun PE, Gehring K. FEBS J. 274, 1600-9, (2007). View articlePMID: 17480208

2.Structure and mechanism of E. coli RNA 2',3'-cyclic phosphodiesterase. Remus BS, Jacewicz A, Shuman S. RNA 20, 1697-705, (2014). View articlePMID: 25239919

3.Crystal structures of the semireduced and inhibitor-bound forms of cyclic nucleotide phosphodiesterase from Arabidopsis thaliana. Hofmann A, Grella M, Botos I, Filipowicz W, Wlodawer A. J. Biol. Chem. 277, 1419-25, (2002). View articlePMID: 11694509

4.Crystallographic analysis of the reaction cycle of 2',3'-cyclic nucleotide 3'-phosphodiesterase, a unique member of the 2H phosphoesterase family. Myllykoski M, Raasakka A, Lehtimaki M, Han H, Kursula I, Kursula P. J. Mol. Biol. 425, 4307-22, (2013). View articlePMID: 23831225

5.Determinants of ligand binding and catalytic activity in the myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase. Raasakka A, Myllykoski M, Laulumaa S, Lehtimaki M, Hartlein M, Moulin M, Kursula I, Kursula P. Sci Rep 5, 16520, (2015). View articlePMID: 26563764

Cross References

Contributing Member Database Entry
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.