Dataset Information
Glutamine-stabilized filament form of Glutamine Synthetase under turnover conditions
Ontology highlight
ABSTRACT:
SUBMITTER: Eric Raymond Greene
PROVIDER: EMPIAR-13622 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Product-stabilized filamentation by human glutamine synthetase allosterically tunes metabolic activity.
bioRxiv : the preprint server for biology 20250706
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 these filaments, which in turn exhibit reduced catalytic specificity for ammonia at phy ...[more]