Structural Basis for the Differential Regulatory Roles of the PDZ Domain in C-Terminal Processing Proteases.
CTP
PDZ domain
Prc
enzyme activation
mechanisms of action
proteases
Journal
mBio
ISSN: 2150-7511
Titre abrégé: mBio
Pays: United States
ID NLM: 101519231
Informations de publication
Date de publication:
06 08 2019
06 08 2019
Historique:
entrez:
8
8
2019
pubmed:
8
8
2019
medline:
28
4
2020
Statut:
epublish
Résumé
Carboxyl (C)-terminal processing proteases (CTPs) participate in protective and regulatory proteolysis in bacteria. The PDZ domain is central to the activity of CTPs but plays inherently different regulatory roles. For example, the PDZ domain inhibits the activity of the signaling protease CtpB by blocking the active site but is required for the activation of Prc (or Tsp), a tail-specific protease that degrades SsrA-tagged proteins. Here, by structural and functional analyses, we show that in the unliganded resting state of Prc, the PDZ domain is docked inside the bowl-shaped scaffold without contacting the active site, which is kept in a default misaligned conformation. In Prc, a hydrophobic substrate sensor distinct from CtpB engages substrate binding to the PDZ domain and triggers a structural remodeling to align the active-site residues. Therefore, this work reveals the structural basis for understanding the contrasting roles of the PDZ domain in the regulation of CTPs.
Identifiants
pubmed: 31387902
pii: mBio.01129-19
doi: 10.1128/mBio.01129-19
pmc: PMC6686036
pii:
doi:
Substances chimiques
Escherichia coli Proteins
0
FtsI protein, E coli
0
Penicillin-Binding Proteins
0
Peptidoglycan Glycosyltransferase
EC 2.4.1.129
Endopeptidases
EC 3.4.-
C-terminal processing peptidase
EC 3.4.21.102
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2019 Chueh et al.
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