7W85

Structural of the filamentous Escherichia coli glutamine synthetase

これはPDB形式変換不可エントリーです。

7W85 の概要

• エントリーDOI: 10.2210/pdb7w85/pdb
• EMDBエントリー: 32352
• 分子名称: Glutamine synthetase, NICKEL (II) ION (2 entities in total)
• 機能のキーワード: glutamine synthetase, filament, biosynthetic protein
• 由来する生物種: Escherichia coli BL21(DE3)
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 1249663.72

構造登録者

Huang, P.-C.,Chen, S.-K.,Wu, K.-P. (登録日: 2021-12-07, 公開日: 2022-04-06, 最終更新日: 2024-06-26)

主引用文献

Huang, P.C.,Chen, S.K.,Chiang, W.H.,Ho, M.R.,Wu, K.P.
Structural basis for the helical filament formation of Escherichia coli glutamine synthetase.
Protein Sci., 31:e4304-e4304, 2022

PubMed Abstract: Escherichia coli glutamine synthetase (EcGS) spontaneously forms a dodecamer that catalytically converts glutamate to glutamine. EcGS stacks with other dodecamers to create a filament-like polymer visible under transmission electron microscopy. Filamentous EcGS is induced by environmental metal ions. We used cryo-electron microscopy (cryo-EM) to decipher the structure of metal ion (nickel)-induced EcGS helical filament at a sub-3Å resolution. EcGS filament formation involves stacking of native dodecamers by chelating nickel ions to residues His5 and His13 in the first N-terminal helix (H1). His5 and His13 from paired parallel H1 helices provide salt bridges and hydrogen bonds to tightly stack two dodecamers. One subunit of the EcGS filament hosts two nickel ions, whereas the dodecameric interface and the ATP/Mg-binding site both host a nickel ion each. We reveal that upon adding glutamate or ATP for catalytic reactions, nickel-induced EcGS filament reverts to individual dodecamers. Such tunable filament formation is often associated with stress responses. Our results provide detailed structural information on the mechanism underlying reversible and tunable EcGS filament formation.

PubMed: 35481643
DOI: 10.1002/pro.4304

実験手法

ELECTRON MICROSCOPY (2.94 Å)