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Structural basis for negative regulation of the Escherichia coli maltose system
Open accessPreprint — published as 10.1038/s41467-023-40447-y
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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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Wu, Y., Sun, Y., Richet, E., Han, Z., & Chai, J.
- Affiliations
- University of Cologne (DE)
- Center for Life Sciences (CN)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Chai, Jijie
- Venue
- Research Square
- Published
- 2023-01-13
- OpenAlex
- W4316022674
- Cited by
- 0
- References
- 1
- Type
- posted content
- Language
- en
- Open access
- green
- dx.doi.org
- Locations
- Research Square (acceptedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- malt, negative regulation, transcriptional repression, protein oligomerization, autoinhibition, ADP binding, nucleotide-binding domain, DNA binding, Escherichia coli
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