8BOB

Structural basis for negative regulation of the maltose system

Summary for 8BOB

• Entry DOI: 10.2210/pdb8bob/pdb
• EMDB information: 16140
• Descriptor: Protein MalY, HTH-type transcriptional regulator MalT, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• Functional Keywords: stand, maltose system, transcription, oligomerization
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 4
• Total formula weight: 183355.45

Authors

Chai, J.,Wu, Y. (deposition date: 2022-11-15, release date: 2023-10-18, Last modification date: 2023-10-25)

Primary citation

Wu, Y.,Sun, Y.,Richet, E.,Han, Z.,Chai, J.
Structural basis for negative regulation of the Escherichia coli maltose system.
Nat Commun, 14:4925-4925, 2023

PubMed 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.

PubMed: 37582800
DOI: 10.1038/s41467-023-40447-y

Experimental method

ELECTRON MICROSCOPY (2.94 Å)