About: Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase

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About: Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase 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
has title	Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase
Creator	Zhang, Qi Wang, Guoqiang Gong, Peng Wu, Wei Chen, Zhongzhou Deng, Zengqin Li, Xiaorong Gorbalenya, Alexander Snijder, Eric Feng, Chong Feng, Wenhai Qi, Xiaoxuan Tao, Ye Yu, Lin Zhang, Xingliang Lehmann, Kathleen Posthuma, Clara
Source	Medline; PMC
abstract	All positive-stranded RNA viruses with genomes >∼7 kb encode helicases, which generally are poorly characterized. The core of the nidovirus superfamily 1 helicase (HEL1) is associated with a unique N-terminal zinc-binding domain (ZBD) that was previously implicated in helicase regulation, genome replication and subgenomic mRNA synthesis. The high-resolution structure of the arterivirus helicase (nsp10), alone and in complex with a polynucleotide substrate, now provides first insights into the structural basis for nidovirus helicase function. A previously uncharacterized domain 1B connects HEL1 domains 1A and 2A to a long linker of ZBD, which further consists of a novel RING-like module and treble-clef zinc finger, together coordinating three Zn atoms. On substrate binding, major conformational changes were evident outside the HEL1 domains, notably in domain 1B. Structural characterization, mutagenesis and biochemistry revealed that helicase activity depends on the extensive relay of interactions between the ZBD and HEL1 domains. The arterivirus helicase structurally resembles the cellular Upf1 helicase, suggesting that nidoviruses may also use their helicases for post-transcriptional quality control of their large RNA genomes.
has issue date	2013-12-24(xsd:dateTime)
bibo:doi	10.1093/nar/gkt1310
bibo:pmid	24369429
has license	cc-by-nc
sha1sum (hex)	2559cb0b4a2175212495ab7d44d9305db4a06c05
schema:url	https://doi.org/10.1093/nar/gkt1310
resource representing a document's title	Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase
has PubMed Central identifier	PMC3950703
has PubMed identifier	24369429
schema:publication	Nucleic Acids Res
resource representing a document's body	covid:2559cb0b4a2175212495ab7d44d9305db4a06c05#body_text
is schema:about of	named entity 'FUNCTION' named entity 'NONSENSE-MEDIATED MRNA DECAY' named entity 'POLYNUCLEOTIDE' named entity 'POSITIVE' named entity 'STRUCTURAL CHARACTERIZATION' named entity 'GENERALLY' named entity 'ATOMS' named entity 'BASIS' named entity 'TRANSCRIPTIONAL' named entity 'PREVIOUSLY' named entity 'STRUCTURAL' named entity 'LINKER' named entity 'GENOMES' named entity 'ZINC FINGER' named entity 'REVEALED' named entity 'USE' named entity 'INSIGHTS' named entity 'EXTENSIVE' named entity 'ZINC' named entity 'activity' named entity 'interactions' named entity 'RNA' named entity 'replication' named entity 'function' named entity 'COMPLEX' named entity 'N-TERMINAL ' named entity 'HIGH-RESOLUTION' named entity 'POORLY' named entity 'THEIR' named entity 'UPF1' named entity 'CORE' named entity 'OUTSIDE' named entity 'MODULE' named entity 'MUTAGENESIS' named entity 'ARTERIVIRUS' named entity 'ZINC' named entity 'BINDING' named entity 'HELICASE' named entity 'BASIS' named entity 'SUBSTRATE' named entity 'POST' named entity 'STRUCTURE' named entity 'ENCODE' named entity 'DOMAIN' named entity 'PROVIDES' named entity 'RNA' named entity 'CHANGES' named entity 'CHARACTERIZED' named entity 'HEL1' named entity 'NOVEL' named entity 'HELICASE ACTIVITY' named entity 'HELICASES' named entity 'ARTERIVIRUS' named entity 'REGULATION' named entity 'LIKE' named entity 'MAJOR' named entity 'FUNCTION' named entity 'QUALITY CONTROL' named entity 'UNIQUE' named entity 'TREBLE' named entity 'REGULATORY' named entity 'STRUCTURAL' named entity 'DOMAIN' named entity 'HELICASE' named entity 'CELLULAR'

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