7EVT

Crystal structure of the N-terminal degron-truncated human glutamine synthetase

Summary for 7EVT

• Entry DOI: 10.2210/pdb7evt/pdb
• Descriptor: Glutamine synthetase (1 entity in total)
• Functional Keywords: decamer, n-terminal truncated, n-degron, ligase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 10
• Total formula weight: 418560.23

Authors

Chek, M.F.,Kim, S.Y.,Mori, T.,Hakoshima, T. (deposition date: 2021-05-22, release date: 2021-11-10, Last modification date: 2023-11-29)

Primary citation

Chek, M.F.,Kim, S.Y.,Mori, T.,Kojima, H.,Hakoshima, T.
Crystal structure of N-terminal degron-truncated human glutamine synthetase.
Acta Crystallogr.,Sect.F, 77:427-434, 2021

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: 34726182
DOI: 10.1107/S2053230X21010748

Experimental method

X-RAY DIFFRACTION (2.95 Å)