ArticleThe Journal of biological chemistry2013
Structures of the Bacillus subtilis glutamine synthetase dodecamer reveal large intersubunit catalytic conformational changes linked to a unique feedback inhibition mechanism.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 50 citations in OpenAlex.
- Article
- Glutamine Synthetase: Diverse Regulation and Functions of an Ancient Enzyme.Biochemistry · 2025Review
- Syntrophic bacterial and host-microbe interactions in bacterial vaginosis.The ISME journal · 2025Article
- Article
- Differences in regulation mechanisms of glutamine synthetases from methanogenic archaea unveiled by structural investigations.Communications biology · 2024Article
- Design of a sorbitol-activated nitrogen metabolism-dependent regulatory system for redirection of carbon metabolism flow in Bacillus licheniformis.Nucleic acids research · 2023Article
- M. mazei glutamine synthetase and glutamine synthetase-GlnK1 structures reveal enzyme regulation by oligomer modulation.Nature communications · 2023Article
- Glutamine synthetase and GlnR regulate nitrogen metabolism inApplied and environmental microbiology · 2023Article
- Understanding and application of Bacillus nitrogen regulation: A synthetic biology perspective.Journal of advanced research · 2023Review
- Research progress on GlnR-mediated regulation in Actinomycetes.Frontiers in microbiology · 2023Review
- Polyamine and Ethanolamine Metabolism in Bacteria as an Important Component of Nitrogen Assimilation for Survival and Pathogenicity.Medical sciences (Basel, Switzerland) · 2022Review
- Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.Nature communications · 2022Article
- TnMicrobiology spectrum · 2022Article
- Structural basis for the helical filament formation of Escherichia coli glutamine synthetase.Protein science : a publication of the Protein Society · 2022Article
- Structural Insight into the Contributions of the N-Terminus and Key Active-Site Residues to the Catalytic Efficiency of Glutamine Synthetase 2.Biomolecules · 2020Article
- The Encystment-Related MicroRNAs and Its Regulation Molecular Mechanism inInternational journal of molecular sciences · 2020Article
- Protein crystal structure determination with the crystallophore, a nucleating and phasing agent.Journal of applied crystallography · 2019Article
- Discovery of Potential Anti-infective Therapy Targeting Glutamine Synthetase inFrontiers in chemistry · 2019Article
- Variants of theFrontiers in microbiology · 2019Article
- Bioinformatic Exploration of Metal-Binding Proteome of Zoonotic PathogenFrontiers in genetics · 2019Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Glutamine synthetase (GS), which catalyzes the production of glutamine, plays essential roles in nitrogen metabolism. There are two main bacterial GS isoenzymes, GSI-α and GSI-β. GSI-α enzymes, which have not been structurally characterized, are uniquely feedback-inhibited by Gln. To gain insight into GSI-α function, we performed biochemical and cellular studies and obtained structures for all GSI-α catalytic and regulatory states. GSI-α forms a massive 600-kDa dodecameric machine. Unlike other characterized GS, the Bacillus subtilis enzyme undergoes dramatic intersubunit conformational alterations during formation of the transition state. Remarkably, these changes are required for active site construction. Feedback inhibition arises from a hydrogen bond network between Gln, the catalytic glutamate, and the GSI-α-specific residue, Arg(62), from an adjacent subunit. Notably, Arg(62) must be ejected for proper active site reorganization. Consistent with these findings, an R62A mutation abrogates Gln feedback inhibition but does not affect catalysis. Thus, these data reveal a heretofore unseen restructuring of an enzyme active site that is coupled with an isoenzyme-specific regulatory mechanism. This GSI-α-specific regulatory network could be exploited for inhibitor design against Gram-positive pathogens.
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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.