8BOB

Structural basis for negative regulation of the maltose system

8BOB の概要

• エントリーDOI: 10.2210/pdb8bob/pdb
• EMDBエントリー: 16140
• 分子名称: Protein MalY, HTH-type transcriptional regulator MalT, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: stand, maltose system, transcription, oligomerization
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 183355.45

構造登録者

Chai, J.,Wu, Y. (登録日: 2022-11-15, 公開日: 2023-10-18, 最終更新日: 2025-07-09)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (2.94 Å)