ArticleThe EMBO journal2000
Structure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reaction.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 59 citations in OpenAlex.
- An unexpected 2-histidine phosphoesterase activity of suppressor of T-cell receptor signaling protein 1 contributes to the suppression of cell signaling.The Journal of biological chemistry · 2020Article
- Structural basis for the evolution of cyclic phosphodiesterase activity in the U6 snRNA exoribonuclease Usb1.Nucleic acids research · 2020Article
- Atomic structures of the RNA end-healing 5'-OH kinase and 2',3'-cyclic phosphodiesterase domains of fungal tRNA ligase: conformational switches in the kinase upon binding of the GTP phosphate donor.Nucleic acids research · 2019Article
- Structural and mechanistic basis for preferential deadenylation of U6 snRNA by Usb1.Nucleic acids research · 2018Article
- Interaction of 2',3'-cAMP with Rbp47b Plays a Role in Stress Granule Formation.Plant physiology · 2018Article
- Traversing the RNA world.The Journal of biological chemistry · 2017Article
- Crystal structure of the RNA 2',3'-cyclic phosphodiesterase from Deinococcus radiodurans.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Structural basis for 2'-5'-oligoadenylate binding and enzyme activity of a viral RNase L antagonist.Journal of virology · 2015Article
- The natural history of ADP-ribosyltransferases and the ADP-ribosylation system.Current topics in microbiology and immunology · 2015Review
- Unmasking Novel Loci for Internal Phosphorus Utilization Efficiency in Rice Germplasm through Genome-Wide Association Analysis.PloS one · 2015Article
- Structure and mechanism of E. coli RNA 2',3'-cyclic phosphodiesterase.RNA (New York, N.Y.) · 2014Article
- Crystallographic analysis of the reaction cycle of 2',3'-cyclic nucleotide 3'-phosphodiesterase, a unique member of the 2H phosphoesterase family.Journal of molecular biology · 2013Article
- Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases.Nature structural & molecular biology · 2013Article
- C16orf57, a gene mutated in poikiloderma with neutropenia, encodes a putative phosphodiesterase responsible for the U6 snRNA 3' end modification.Genes & development · 2012Article
- Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: active-site ligand binding and molecular conformation.PloS one · 2012Article
- Branchiostoma floridae has separate healing and sealing enzymes for 5'-phosphate RNA ligation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Mammalian 2',3' cyclic nucleotide phosphodiesterase (CNP) can function as a tRNA splicing enzyme in vivo.RNA (New York, N.Y.) · 2008Article
- AKAP18 contains a phosphoesterase domain that binds AMP.Journal of molecular biology · 2008Article
- The structure of Pyrococcus horikoshii 2'-5' RNA ligase at 1.94 A resolution reveals a possible open form with a wider active-site cleft.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- The histone variant mH2A1.1 interferes with transcription by down-regulating PARP-1 enzymatic activity.Genes & development · 2006Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The crystal structure of the cyclic phosphodiesterase (CPDase) from Arabidopsis thaliana, an enzyme involved in the tRNA splicing pathway, was determined at 2.5 A resolution. CPDase hydrolyzes ADP-ribose 1",2"-cyclic phosphate (Appr>p), a product of the tRNA splicing reaction, to the monoester ADP-ribose 1"-phosphate (Appr-1"p). The 181 amino acid protein shows a novel, bilobal arrangement of two alphabeta modules. Each lobe consists of two alpha-helices on the outer side of the molecule, framing a three- or four-stranded antiparallel beta-sheet in the core of the protein. The active site is formed at the interface of the two beta-sheets in a water-filled cavity involving residues from two H-X-T/S-X motifs. This previously noticed motif participates in coordination of a sulfate ion. A solvent-exposed surface loop (residues 100-115) is very likely to play a flap-like role, opening and closing the active site. Based on the crystal structure and on recent mutagenesis studies of a homologous CPDase from Saccharomyces cerevisiae, we propose an enzymatic mechanism that employs the nucleophilic attack of a water molecule activated by one of the active site histidines.
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