{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chek MF"],"funding":["Takeda Science Foundation","Japan Agency for Medical Research and Development","Ministry of Education, Culture, Sports, Science and Technology"],"pagination":["427-434"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8561813"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["77(Pt 11)"],"pubmed_abstract":["Glutamine synthetase (GS) is a decameric enzyme that plays a key role in nitrogen metabolism. Acetylation of the N-terminal degron (N-degron) of GS is essential for ubiquitylation and subsequent GS degradation. The full-length GS structure showed that the N-degron is buried inside the GS decamer and is inaccessible to the acetyltransferase. The structure of N-degron-truncated GS reported here reveals that the N-degron is not essential for GS decamer formation. It is also shown that the N-degron can be exposed to a solvent region through a series of conformational adjustments upon ligand binding. In summary, this study elucidated the dynamic movement of the N-degron and the possible effect of glutamine in enhancing the acetylation process."],"journal":["Acta crystallographica. Section F, Structural biology communications"],"pubmed_title":["Crystal structure of N-terminal degron-truncated human glutamine synthetase."],"pmcid":["PMC8561813"],"funding_grant_id":["JP17gm1010008"],"pubmed_authors":["Kim SY","Chek MF","Kojima H","Mori T","Hakoshima T"],"additional_accession":[]},"is_claimable":false,"name":"Crystal structure of N-terminal degron-truncated human glutamine synthetase.","description":"Glutamine synthetase (GS) is a decameric enzyme that plays a key role in nitrogen metabolism. Acetylation of the N-terminal degron (N-degron) of GS is essential for ubiquitylation and subsequent GS degradation. The full-length GS structure showed that the N-degron is buried inside the GS decamer and is inaccessible to the acetyltransferase. The structure of N-degron-truncated GS reported here reveals that the N-degron is not essential for GS decamer formation. It is also shown that the N-degron can be exposed to a solvent region through a series of conformational adjustments upon ligand binding. In summary, this study elucidated the dynamic movement of the N-degron and the possible effect of glutamine in enhancing the acetylation process.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Nov","modification":"2026-05-31T16:01:47.755Z","creation":"2025-02-19T01:27:31.549Z"},"accession":"S-EPMC8561813","cross_references":{"pubmed":["34726182"],"doi":["10.1107/s2053230x21010748","10.1107/S2053230X21010748"]}}