<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Chek MF</submitter><funding>Takeda Science Foundation</funding><funding>Japan Agency for Medical Research and Development</funding><funding>Ministry of Education, Culture, Sports, Science and Technology</funding><pagination>427-434</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8561813</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>77(Pt 11)</volume><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.</pubmed_abstract><journal>Acta crystallographica. Section F, Structural biology communications</journal><pubmed_title>Crystal structure of N-terminal degron-truncated human glutamine synthetase.</pubmed_title><pmcid>PMC8561813</pmcid><funding_grant_id>JP17gm1010008</funding_grant_id><pubmed_authors>Kim SY</pubmed_authors><pubmed_authors>Chek MF</pubmed_authors><pubmed_authors>Kojima H</pubmed_authors><pubmed_authors>Mori T</pubmed_authors><pubmed_authors>Hakoshima T</pubmed_authors></additional><is_claimable>false</is_claimable><name>Crystal structure of N-terminal degron-truncated human glutamine synthetase.</name><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.</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Nov</publication><modification>2026-05-31T16:01:47.755Z</modification><creation>2025-02-19T01:27:31.549Z</creation></dates><accession>S-EPMC8561813</accession><cross_references><pubmed>34726182</pubmed><doi>10.1107/s2053230x21010748</doi><doi>10.1107/S2053230X21010748</doi></cross_references></HashMap>