The structural basis for deubiquitination by the fingerless USP-type effector TssM.
Journal
Life science alliance
ISSN: 2575-1077
Titre abrégé: Life Sci Alliance
Pays: United States
ID NLM: 101728869
Informations de publication
Date de publication:
Feb 2024
Feb 2024
Historique:
received:
06
10
2023
revised:
28
11
2023
accepted:
29
11
2023
medline:
4
1
2024
pubmed:
4
1
2024
entrez:
3
1
2024
Statut:
epublish
Résumé
Intracellular bacteria are threatened by ubiquitin-mediated autophagy, whenever the bacterial surface or enclosing membrane structures become targets of host ubiquitin ligases. As a countermeasure, many intracellular pathogens encode deubiquitinase (DUB) effectors to keep their surfaces free of ubiquitin. Most bacterial DUBs belong to the OTU or CE-clan families. The betaproteobacteria
Identifiants
pubmed: 38170641
pii: 7/2/e202302422
doi: 10.26508/lsa.202302422
pii:
doi:
Banques de données
PDB
['2AYO', '3O65', '3VYP', '4UIC', '6NFR', '3TUR', '1UBQ', '8PZ3', '8Q00']
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2023 Hermanns et al.