ArticleJournal of molecular biology2013
Crystallographic analysis of the reaction cycle of 2',3'-cyclic nucleotide 3'-phosphodiesterase, a unique member of the 2H phosphoesterase family.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 20 citations in OpenAlex.
- Nanobodies against the myelin enzyme CNPase as tools for structural and functional studies.Journal of neurochemistry · 2025Article
- Nanobodies against the myelin enzyme CNPase as tools for structural and functional studies.bioRxiv : the preprint server for biology · 2024Article
- Structural basis for the evolution of cyclic phosphodiesterase activity in the U6 snRNA exoribonuclease Usb1.Nucleic acids research · 2020Article
- Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease.Cells · 2020Review
- Generation of 2',3'-Cyclic Phosphate-Containing RNAs as a Hidden Layer of the Transcriptome.Frontiers in genetics · 2018Review
- Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase.BMC biochemistry · 2017Article
- Crystal structure of the RNA 2',3'-cyclic phosphodiesterase from Deinococcus radiodurans.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Antagonistic Functions of MBP and CNP Establish Cytosolic Channels in CNS Myelin.Cell reports · 2017Article
- Article
- Malonate in the nucleotide-binding site traps human AKAP18γ/δ in a novel conformational state.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Determinants of ligand binding and catalytic activity in the myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase.Scientific reports · 2015Article
- Structural basis for 2'-5'-oligoadenylate binding and enzyme activity of a viral RNase L antagonist.Journal of virology · 2015Article
- The myelin membrane-associated enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase: on a highway to structure and function.Neuroscience bulletin · 2014Review
- Structure and mechanism of E. coli RNA 2',3'-cyclic phosphodiesterase.RNA (New York, N.Y.) · 2014Article
- Identification of phosphorylated form of 2', 3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) as 46 kDa phosphoprotein in brain non-synaptic mitochondria overloaded by calcium.Journal of bioenergetics and biomembranes · 2014Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
2H phosphoesterases catalyze reactions on nucleotide substrates and contain two conserved histidine residues in the active site. Very limited information is currently available on the details of the active site and substrate/product binding during the catalytic cycle of these enzymes. We performed a comprehensive X-ray crystallographic study of mouse 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase), a membrane-associated enzyme present at high levels in the tetrapod myelin sheath. We determined crystal structures of the CNPase phosphodiesterase domain complexed with substrate, product, and phosphorothioate analogues. The data provide detailed information on the CNPase reaction mechanism, including substrate binding mode and coordination of the nucleophilic water molecule. Linked to the reaction, an open/close motion of the β5-α7 loop is observed. The role of the N terminus of helix α7--unique for CNPase in the 2H family--during the reaction indicates that 2H phosphoesterases differ in their respective reaction mechanisms despite the conserved catalytic residues. Furthermore, based on small-angle X-ray scattering, we present a model for the full-length enzyme, indicating that the two domains of CNPase form an elongated molecule. Finally, based on our structural data and a comprehensive bioinformatics study, we discuss the conservation of CNPase in various organisms.
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