About: Histidine Triad-Like Motif of the Rotavirus NSP2 Octamer Mediates Both RTPase and NTPase Activities

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Histidine Triad-Like Motif of the Rotavirus NSP2 Octamer Mediates Both RTPase and NTPase Activities Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Histidine Triad-Like Motif of the Rotavirus NSP2 Octamer Mediates Both RTPase and NTPase Activities
Creator	Riadi, Gonzalo Patton, John Carpio, Gonzalez-Nilo, Fernando Taraporewala, Zenobia Vasquez-Del, Rodrigo
source	Elsevier; Medline; PMC
abstract	Rotavirus NSP2 is an abundant nonstructural RNA-binding protein essential for forming the viral factories that support replication of the double-stranded RNA genome. NSP2 exists as stable doughnut-shaped octamers within the infected cell, representing the tail-to-tail interaction of two tetramers. Extending diagonally across the surface of each octamer are four highly basic grooves that function as binding sites for single-stranded RNA. Between the N and C-terminal domains of each monomer is a deep electropositive cleft containing a catalytic site that hydrolyzes the γ-β phosphoanhydride bond of any NTP. The catalytic site has similarity to those of the histidine triad (HIT) family of nucleotide-binding proteins. Due to the close proximity of the grooves and clefts, we investigated the possibility that the RNA-binding activity of the groove promoted the insertion of the 5′-triphosphate moiety of the RNA into the cleft, and the subsequent hydrolysis of its γ-β phosphoanhydride bond. Our results show that NSP2 hydrolyzes the γP from RNAs and NTPs through Mg(2+)-dependent activities that proceed with similar reaction velocities, that require the catalytic His(225) residue, and that produce a phosphorylated intermediate. Competition assays indicate that although both substrates enter the active site, RNA is the preferred substrate due to its higher affinity for the octamer. The RTPase activity of NSP2 may account for the absence of 5′-terminal γP on the (−) strands of the dsRNA genome segments. This is the first report of a HIT-like protein with a multifunctional catalytic site, capable of accommodating both NTPs and RNAs during γP hydrolysis.
has issue date	2006-09-01(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2006.07.050
bibo:pmid	16934294
has license	green-oa
sha1sum (hex)	d81a5153031b645b3606f780c6a9fb6a8b2283a9
schema:url	https://doi.org/10.1016/j.jmb.2006.07.050
resource representing a document's title	Histidine Triad-Like Motif of the Rotavirus NSP2 Octamer Mediates Both RTPase and NTPase Activities
has PubMed Central identifier	PMC1924841
has PubMed identifier	16934294
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:d81a5153031b645b3606f780c6a9fb6a8b2283a9#body_text
is schema:about of	named entity 'MOTIF' named entity 'basic' named entity 'highly' named entity 'bond' named entity 'diagonally' named entity 'hydrolysis' named entity 'bond' named entity 'RNAs' named entity 'LIKE' named entity 'ROTAVIRUS' named entity 'MEDIATES' named entity 'PRODUCE' named entity 'DEEP' named entity 'DOUGHNUT' named entity 'BINDING ACTIVITY' named entity 'IS A' named entity 'TAIL' named entity 'FACTORIES' named entity 'ACTIVITIES' named entity 'DSRNA' named entity 'LIKE' named entity 'RESULTS' named entity 'NSP2' named entity 'SIMILARITY' named entity 'NUCLEOTIDE' named entity 'FAMILY' named entity 'ACROSS' named entity 'RNA' named entity 'VELOCITIES' named entity '225' named entity 'NTPASE' named entity 'STABLE' named entity 'CATALYTIC SITE' named entity 'INSERTION' named entity 'GROOVE' named entity 'ACTIVE SITE' named entity 'ENTER' named entity 'ACTIVITIES' named entity 'HISTIDINE' named entity 'NSP2' named entity 'TRIAD' named entity 'PHOSPHORYLATED' named entity 'INVESTIGATED' named entity 'DOUBLE-STRANDED RNA' named entity 'REPORT' named entity 'AFFINITY' named entity 'BASIC' named entity 'BINDING PROTEIN' named entity 'BOND' named entity 'POSSIBILITY' named entity 'SEGMENTS' named entity 'CONTAINING' named entity 'BINDING SITES' named entity 'DUE TO' named entity 'ABUNDANT' named entity 'TERMINAL' named entity 'MONOMER' named entity 'HIGHLY' named entity 'INTERMEDIATE' named entity 'ABSENCE OF' named entity 'NTP' named entity 'CLEFT' named entity 'FUNCTION' named entity 'OF EACH' named entity 'SUBSEQUENT' named entity 'PREFERRED' named entity 'REPLICATION' named entity 'PROXIMITY' named entity 'TRIAD' named entity 'TRIPHOSPHATE' named entity 'HIT' named entity 'SUPPORT' named entity 'CATALYTIC' named entity 'ACTIVITY' named entity '80%' named entity 'CLOSE'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software