7EVT

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

7EVT の概要

• エントリーDOI: 10.2210/pdb7evt/pdb
• 分子名称: Glutamine synthetase (1 entity in total)
• 機能のキーワード: decamer, n-terminal truncated, n-degron, ligase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 418560.23

構造登録者

Chek, M.F.,Kim, S.Y.,Mori, T.,Hakoshima, T. (登録日: 2021-05-22, 公開日: 2021-11-10, 最終更新日: 2023-11-29)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.95 Å)