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-Structure paper
Title | Product-stabilized filamentation by human glutamine synthetase allosterically tunes metabolic activity |
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Journal, issue, pages | To Be Published |
Publish date | May 27, 2025 (structure data deposition date) |
![]() | Greene ER / Muniz RS / Yamamura H / Hoff S / Bajaj P / Lee DJ / Thompson EM / Arada A / Bonomi M / Kollman JM / Fraser JS |
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Methods | EM (single particle) |
Resolution | 1.95 - 2.27 Å |
Structure data | EMDB-70841, PDB-9otm: EMDB-70842, PDB-9otn: EMDB-70843, PDB-9oto: EMDB-70844, PDB-9otp: EMDB-70845, PDB-9otq: |
Chemicals | ![]() ChemComp-ATP: ![]() ChemComp-MG: ![]() ChemComp-GLN: ![]() ChemComp-ADP: |
Source |
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![]() | LIGASE / Glutamine synthetase / glutamate-ammonia ligase / filament / Type II / turnover conditions |