ArticleProtein science : a publication of the Protein Society2022
Structural basis for the helical filament formation of Escherichia coli glutamine synthetase.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Product-stabilized filamentation by human glutamine synthetase allosterically tunes metabolic activity.eLife · 2026Article
- Glutamine metabolic enzymes: to filament or not to filament?Biochemical Society transactions · 2026Review
- Structural diversity and oligomerization of bacterial ubiquitin-like proteins.Structure (London, England : 1993) · 2025Article
- Article
- Nucleotide-induced hyper-oligomerization inactivates transcription termination factor ρ.Nature communications · 2025Article
- Glutamine Synthetase: Diverse Regulation and Functions of an Ancient Enzyme.Biochemistry · 2025Review
- Article
- Structural diversity and oligomerization of bacterial ubiquitin-like proteins.bioRxiv : the preprint server for biology · 2024Article
- Greater than the sum of parts: Mechanisms of metabolic regulation by enzyme filaments.Current opinion in structural biology · 2023Review
- Structural basis for the helical filament formation of Escherichia coli glutamine synthetase.Protein science : a publication of the Protein Society · 2022Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli glutamine synthetase (EcGS) spontaneously forms a dodecamer that catalytically converts glutamate to glutamine. EcGS stacks with other dodecamers to create a filament-like polymer visible under transmission electron microscopy. Filamentous EcGS is induced by environmental metal ions. We used cryo-electron microscopy (cryo-EM) to decipher the structure of metal ion (nickel)-induced EcGS helical filament at a sub-3Å resolution. EcGS filament formation involves stacking of native dodecamers by chelating nickel ions to residues His5 and His13 in the first N-terminal helix (H1). His5 and His13 from paired parallel H1 helices provide salt bridges and hydrogen bonds to tightly stack two dodecamers. One subunit of the EcGS filament hosts two nickel ions, whereas the dodecameric interface and the ATP/Mg-binding site both host a nickel ion each. We reveal that upon adding glutamate or ATP for catalytic reactions, nickel-induced EcGS filament reverts to individual dodecamers. Such tunable filament formation is often associated with stress responses. Our results provide detailed structural information on the mechanism underlying reversible and tunable EcGS filament formation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.