7A1D

Cryo-EM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis (open conformation)

7A1D の概要

• エントリーDOI: 10.2210/pdb7a1d/pdb
• EMDBエントリー: 11606
• 分子名称: NAD-specific glutamate dehydrogenase (1 entity in total)
• 機能のキーワード: large glutamate dehydrogenase mycobacterium metabolism, oxidoreductase
• 由来する生物種: Mycolicibacterium smegmatis MC2 155
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 705367.44

構造登録者

Lazaro, M.,Melero, R.,Huet, C.,Lopez-Alonso, J.P.,Delgado, S.,Dodu, A.,Bruch, E.M.,Abriata, L.A.,Alzari, P.M.,Valle, M.,Lisa, M.N. (登録日: 2020-08-12, 公開日: 2021-06-09, 最終更新日: 2025-05-14)

主引用文献

Lazaro, M.,Melero, R.,Huet, C.,Lopez-Alonso, J.P.,Delgado, S.,Dodu, A.,Bruch, E.M.,Abriata, L.A.,Alzari, P.M.,Valle, M.,Lisa, M.N.
3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme.
Commun Biol, 4:684-684, 2021

PubMed Abstract: Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate dehydrogenases composed of 180 kDa subunits (L-GDHs) contain long N- and C-terminal segments flanking the catalytic core. Despite the relevance of L-GDHs in bacterial physiology, the lack of structural data for these enzymes has limited the progress of functional studies. Here we show that the mycobacterial L-GDH (mL-GDH) adopts a quaternary structure that is radically different from that of related low molecular weight enzymes. Intersubunit contacts in mL-GDH involve a C-terminal domain that we propose as a new fold and a flexible N-terminal segment comprising ACT-like and PAS-type domains that could act as metabolic sensors for allosteric regulation. These findings uncover unique aspects of the structure-function relationship in the subfamily of L-GDHs.

PubMed: 34083757
DOI: 10.1038/s42003-021-02222-x

実験手法

ELECTRON MICROSCOPY (4.19 Å)