Turnip yellow mosaic virus protease binds ubiquitin suboptimally to fine-tune its deubiquitinase activity.
crystal structure
deubiquitylation (deubiquitination)
plant virus
plus-stranded RNA virus
protein complex
ubiquitin
viral protease
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
02 10 2020
02 10 2020
Historique:
received:
01
06
2020
revised:
27
07
2020
pubmed:
1
8
2020
medline:
4
2
2021
entrez:
1
8
2020
Statut:
ppublish
Résumé
Single-stranded, positive-sense RNA viruses assemble their replication complexes in infected cells from a multidomain replication polyprotein. This polyprotein usually contains at least one protease, the primary function of which is to process the polyprotein into mature proteins. Such proteases also may have other functions in the replication cycle. For instance, cysteine proteases (PRO) frequently double up as ubiquitin hydrolases (DUB), thus interfering with cellular processes critical for virus replication. We previously reported the crystal structures of such a PRO/DUB from
Identifiants
pubmed: 32732284
pii: S0021-9258(17)49827-9
doi: 10.1074/jbc.RA120.014628
pmc: PMC7535911
pii:
doi:
Substances chimiques
Ubiquitin
0
Viral Proteins
0
Peptide Hydrolases
EC 3.4.-
Deubiquitinating Enzymes
EC 3.4.19.12
Banques de données
PDB
['4A5U', '1UBQ', '2G45', '5WFI', '4MM3', '4RF1', '4IUM', '3PHW', '4HXD', '3BY4', '4BOS', '5LW5']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
13769-13783Informations de copyright
© 2020 Fieulaine et al.
Déclaration de conflit d'intérêts
Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.
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