About: Crystallographic Analysis of the Reaction Cycle of 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase, a Unique Member of the 2H Phosphoesterase Family

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About: Crystallographic Analysis of the Reaction Cycle of 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase, a Unique Member of the 2H Phosphoesterase Family Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Crystallographic Analysis of the Reaction Cycle of 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase, a Unique Member of the 2H Phosphoesterase Family
Creator	Han, Huijong Kursula, Inari Kursula, Petri Lehtimäki, Mari Myllykoski, Matti Raasakka, Arne
Source	Elsevier; Medline; PMC
abstract	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.
has issue date	2013-11-15(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2013.06.012
bibo:pmid	23831225
has license	els-covid
sha1sum (hex)	8d852e1ab4ff5a384773c0a02ab5572811e1ff5d
schema:url	https://doi.org/10.1016/j.jmb.2013.06.012
resource representing a document's title	Crystallographic Analysis of the Reaction Cycle of 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase, a Unique Member of the 2H Phosphoesterase Family
has PubMed Central identifier	PMC7094350
has PubMed identifier	23831225
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:8d852e1ab4ff5a384773c0a02ab5572811e1ff5d#body_text
is schema:about of	named entity 'CYCLIC NUCLEOTIDE' named entity 'binding' named entity 'reaction' named entity 'substrate' named entity 'domain' named entity 'crystallographic' named entity '80%' named entity 'LENGTH' named entity 'CYCLE' named entity 'CONSERVATION' named entity 'HIGH' named entity 'CNPASE' named entity 'INCLUDING' named entity 'BIOINFORMATICS' named entity 'ELONGATED' named entity 'COMPREHENSIVE' named entity 'STUDY' named entity 'TERMINUS' named entity 'OUR' named entity 'ACTIVE SITE' named entity 'INDICATING' named entity 'CONSERVED' named entity 'B17' named entity 'PRESENT' named entity 'FORM' named entity 'DOMAIN' named entity 'LOOP' named entity 'DETERMINED' named entity 'SUBSTRATE' named entity 'CYCLE' named entity 'PHOSPHOROTHIOATE' named entity 'UNIQUE' named entity 'MODEL' named entity 'INFORMATION' named entity 'ROLE' named entity 'LEVELS' named entity 'MODE' named entity 'PERFORMED' named entity 'CURRENTLY' named entity '80%' named entity 'UNIQUE' named entity 'ANALYSIS' named entity 'CYCLIC NUCLEOTIDE' named entity 'THESE' named entity 'MECHANISMS' named entity 'MEMBER OF' named entity 'SMALL-ANGLE X-RAY SCATTERING' named entity 'CRYSTAL' named entity 'BASED' named entity 'BINDING' named entity 'DISCUSS' named entity 'PHOSPHODIESTERASE' named entity 'REACTION' named entity 'FAMILY' named entity 'B25' named entity 'THEIR' named entity 'PRODUCT' named entity 'MYELIN SHEATH' named entity 'AVAILABLE' named entity 'STRUCTURAL DATA' named entity 'WATER MOLECULE' named entity 'HISTIDINE' named entity 'COORDINATION' named entity 'CATALYTIC' named entity 'ENZYMES' named entity 'VARIOUS' named entity 'HELIX' named entity 'ENZYME' named entity 'TETRAPOD' named entity 'STRUCTURES' named entity 'PHOSPHODIESTERASE' named entity 'VERY LIMITED' named entity 'REACTION MECHANISM' named entity 'CONTAIN' named entity 'FAMILY' named entity 'REACTION'

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