Snapshots of ADP-ribose bound to Getah virus macro domain reveal an intriguing choreography.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
02 09 2020
02 09 2020
Historique:
received:
17
05
2020
accepted:
29
07
2020
entrez:
4
9
2020
pubmed:
4
9
2020
medline:
3
3
2021
Statut:
epublish
Résumé
Alphaviruses are (re-)emerging arboviruses of public health concern. The nsP3 gene product is one of the key players during viral replication. NsP3 comprises three domains: a macro domain, a zinc-binding domain and a hypervariable region. The macro domain is essential at both early and late stages of the replication cycle through ADP-ribose (ADPr) binding and de-ADP-ribosylation of host proteins. However, both its specific role and the precise molecular mechanism of de-ADP-ribosylation across specific viral families remains to be elucidated. Here we investigate by X-ray crystallography the mechanism of ADPr reactivity in the active site of Getah virus macro domain, which displays a peculiar substitution of one of the conserved residues in the catalytic loop. ADPr adopts distinct poses including a covalent bond between the C''1 of the ADPr and a conserved Togaviridae-specific cysteine. These different poses observed for ADPr may represent snapshots of the de-ADP-ribosylation mechanism, highlighting residues to be further characterised.
Identifiants
pubmed: 32879358
doi: 10.1038/s41598-020-70870-w
pii: 10.1038/s41598-020-70870-w
pmc: PMC7468284
doi:
Substances chimiques
Viral Nonstructural Proteins
0
Adenosine Diphosphate Ribose
20762-30-5
Viral Proteases
EC 3.4.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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