ArticleNature communications2023
Structural basis for negative regulation of the Escherichia coli maltose system.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- Developing hybrid thiomaltodextrins as specific ligands to the maltodextrin transporter ofRSC advances · 2026Article
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- A bacterial CARD-NLR-like immune system controls the release of gene transfer agents.Nature microbiology · 2026Article
- Molecular Strategies of Carbohydrate Binding to Intrinsically Disordered Regions in Bacterial Transcription Factors.International journal of molecular sciences · 2026Article
- Diverse bacterial pattern recognition receptors sense the conserved phage proteome.bioRxiv : the preprint server for biology · 2026Article
- Structural insights into transcription activation of theiScience · 2024Article
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- Microbial β C-S Lyases: Enzymes with Multifaceted Roles in Flavor Generation.International journal of molecular sciences · 2024Review
- Structural and functional characterization of AfsR, an SARP family transcriptional activator of antibiotic biosynthesis in Streptomyces.PLoS biology · 2024Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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