Article
Product-stabilized filamentation by human glutamine synthetase allosterically tunes metabolic activity
2025-07-06
Abstract excerpt
To maintain metabolic homeostasis, enzymes must adapt to fluctuating nutrient levels through mechanisms beyond gene expression. Here, we demonstrate that human glutamine synthetase (GS) can reversibly polymerize into filaments aided by a composite binding site formed at the filament interface by the product, glutamine. Time-resolved cryo-electron microscopy (cryo-EM) confirms that glutamine binding stabilizes thes...
Topics
Open a Topic to create a Post that cites this publication.
Identifiers and source
- Literature Corpus work
- e6d46a40-2a90-5cf0-8405-5999c152e6b5
- DOI
- 10.1101/2025.07.04.663231
