Structural basis for negative regulation of the Escherichia coli maltose system.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
15 08 2023
15 08 2023
Historique:
received:
18
12
2022
accepted:
26
07
2023
medline:
17
8
2023
pubmed:
16
8
2023
entrez:
15
8
2023
Statut:
epublish
Résumé
Proteins from the signal transduction ATPases with numerous domains (STAND) family are known to play an important role in innate immunity. However, it remains less well understood how they function in transcriptional regulation. MalT is a bacterial STAND that controls the Escherichia coli maltose system. Inactive MalT is sequestered by different inhibitory proteins such as MalY. Here, we show that MalY interacts with one oligomerization interface of MalT to form a 2:2 complex. MalY represses MalT activity by blocking its oligomerization and strengthening ADP-mediated MalT autoinhibition. A loop region N-terminal to the nucleotide-binding domain (NBD) of MalT has a dual role in mediating MalT autoinhibition and activation. Structural comparison shows that ligand-binding induced oligomerization is required for stabilizing the C-terminal domains and conferring DNA-binding activity. Together, our study reveals the mechanism whereby a prokaryotic STAND is inhibited by a repressor protein and offers insights into signaling by STAND transcription activators.
Identifiants
pubmed: 37582800
doi: 10.1038/s41467-023-40447-y
pii: 10.1038/s41467-023-40447-y
pmc: PMC10427625
doi:
Substances chimiques
Maltose
69-79-4
DNA-Binding Proteins
0
Escherichia coli Proteins
0
Transcription Factors
0
Bacterial Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4925Informations de copyright
© 2023. Springer Nature Limited.
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